1000 Sentences With "acceptor" | Random Sentence Generator

" The creatures that live in ODZs, she said, "have to use other elements that act as an electron acceptor to extract energy from food.

Philadelphia (CNN)Bill Clinton's history of speeches at the Democratic National Convention has been like his political career, a series of ups and downs, where the former president has played the role of validator, acceptor and character witness.

Phytoene desaturase (3,4-didehydrolycopene-forming) (, 5-step phytoene desaturase, five-step phytoene desaturase, phytoene desaturase (ambiguous), Al-1) is an enzyme with systematic name 15-cis-phytoene:acceptor oxidoreductase (3,4-didehydrolycopene-forming). This enzyme catalyses the following chemical reaction : 15-cis-phytoene + 5 acceptor \rightleftharpoons all-trans-3,4-didehydrolycopene + 5 reduced acceptor (overall reaction) : (1a) 15-cis-phytoene + acceptor \rightleftharpoons all-trans-phytofluene + reduced acceptor : (1b) all-trans-phytofluene + acceptor \rightleftharpoons all-trans- zeta-carotene + reduced acceptor : (1c) all-trans-zeta-carotene + acceptor \rightleftharpoons all-trans-neurosporene + reduced acceptor : (1d) all-trans- neurosporene + acceptor \rightleftharpoons all-trans-lycopene + reduced acceptor : (1e) all-trans-lycopene + acceptor \rightleftharpoons all- trans-3,4-didehydrolycopene + reduced acceptor This enzyme is involved in carotenoid biosynthesis.

Phytoene desaturase (neurosporene-forming) (, 3-step phytoene desaturase, three-step phytoene desaturase, phytoene desaturase (ambiguous), CrtI (ambiguous)) is an enzyme with systematic name 15-cis-phytoene:acceptor oxidoreductase (neurosporene-forming). This enzyme catalyses the following chemical reaction : 15-cis-phytoene + 3 acceptor \rightleftharpoons all-trans- neurosporene + 3 reduced acceptor (overall reaction) : (1a) 15-cis-phytoene + acceptor \rightleftharpoons all-trans-phytofluene + reduced acceptor : (1b) all-trans-phytofluene + acceptor \rightleftharpoons all-trans-zeta-carotene + reduced acceptor : (1c) all-trans-zeta-carotene + acceptor \rightleftharpoons all-trans-neurosporene + reduced acceptor This enzyme is involved in carotenoid biosynthesis.

In enzymology, a selenate reductase () is an enzyme that catalyzes the chemical reaction :selenite + H2O + acceptor \rightleftharpoons selenate + reduced acceptor The 3 substrates of this enzyme are selenite, H2O, and acceptor, whereas its two products are selenate and reduced acceptor. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is selenite:reduced acceptor oxidoreductase.

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out). NADH + acceptor = NAD+ + reduced acceptor.

Phytoene desaturase (zeta-carotene-forming) (, CrtIa, 2-step phytoene desaturase (ambiguous), two-step phytoene desaturase (ambiguous)) is an enzyme with systematic name 15-cis-phytoene:acceptor oxidoreductase (zeta-carotene- forming). This enzyme catalyses the following chemical reaction : 15-cis- phytoene + 2 acceptor \rightleftharpoons all-trans-zeta-carotene + 2 reduced acceptor (overall reaction) : (1a) 15-cis-phytoene + acceptor \rightleftharpoons all-trans-phytofluene + reduced acceptor : (1b) all-trans- phytofluene + acceptor \rightleftharpoons all-trans-zeta-carotene + reduced acceptor The enzyme is involved in carotenoid biosynthesis.

In enzymology, a hydroxylamine reductase () is an enzyme that catalyzes the chemical reaction :NH3 \+ H2O + acceptor \rightleftharpoons hydroxylamine + reduced acceptor The 3 substrates of this enzyme are NH3, H2O, and acceptor, whereas its two products are hydroxylamine and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with other acceptors. The systematic name of this enzyme class is ammonia:acceptor oxidoreductase. Other names in common use include hydroxylamine (acceptor) reductase, and ammonia:(acceptor) oxidoreductase.

In enzymology, a glycerol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :glycerol + acceptor \rightleftharpoons glycerone + reduced acceptor Thus, the two substrates of this enzyme are glycerol and acceptor, whereas its two products are glycerone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is glycerol:acceptor 1-oxidoreductase. This enzyme is also called glycerol:(acceptor) 1-oxidoreductase.

Carvone reductase () is an enzyme with systematic name (+)-dihydrocarvone:acceptor 1,6-oxidoreductase. This enzyme catalyses the following chemical reaction : (1) (+)-dihydrocarvone + acceptor \rightleftharpoons (-)-carvone + reduced acceptor : (2) (-)-isodihydrocarvone + acceptor \rightleftharpoons (+)-carvone + reduced acceptor This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14.

All-trans-zeta-carotene desaturase (, Crtlb, phytoene desaturase (ambiguous), 2-step phytoene desaturase (ambiguous), two-step phytoene desaturase (ambiguous), CrtI (ambiguous)) is an enzyme with systematic name all-trans- zeta-carotene:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : all-trans-zeta-carotene + 2 acceptor \rightleftharpoons all-trans-lycopene + 2 reduced acceptor (overall reaction) : (1a) all-trans- zeta-carotene + acceptor \rightleftharpoons all-trans-neurosporene + reduced acceptor : (1b) all-trans-neurosporene + acceptor \rightleftharpoons all- trans-lycopene + reduced acceptor This enzyme is involved in carotenoid biosynthesis.

In enzymology, a selenocysteine lyase (SCL) () is an enzyme that catalyzes the chemical reaction :L-selenocysteine + reduced acceptor \rightleftharpoons selenide + L-alanine + acceptor Thus, the two substrates of this enzyme are L-selenocysteine and reduced acceptor, whereas its 3 products are selenide, L-alanine, and acceptor. This enzyme employs one cofactor, pyridoxal phosphate.

One method of measuring FRET efficiency is to measure the variation in acceptor emission intensity. When the donor and acceptor are in proximity (1–10 nm) due to the interaction of the two molecules, the acceptor emission will increase because of the intermolecular FRET from the donor to the acceptor. For monitoring protein conformational changes, the target protein is labeled with a donor and an acceptor at two loci. When a twist or bend of the protein brings the change in the distance or relative orientation of the donor and acceptor, FRET change is observed.

In enzymology, an alkan-1-ol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :primary alcohol + acceptor \rightleftharpoons aldehyde + reduced acceptor Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is alkan-1-ol:acceptor oxidoreductase. Other names in common use include polyethylene glycol dehydrogenase, and alkan-1-ol:(acceptor) oxidoreductase.

In enzymology, a choline dehydrogenase () is an enzyme that catalyzes the chemical reaction :choline + acceptor \rightleftharpoons betaine aldehyde + reduced acceptor Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products are betaine aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase.

In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :polyvinyl alcohol + acceptor \rightleftharpoons oxidized polyvinyl alcohol + reduced acceptor Thus, the two substrates of this enzyme are polyvinyl alcohol and acceptor, whereas its two products are oxidized polyvinyl alcohol and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with other acceptors. The systematic name of this enzyme class is polyvinyl-alcohol:acceptor oxidoreductase. Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase.

In enzymology, a D-sorbitol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :D-sorbitol + acceptor \rightleftharpoons L-sorbose + reduced acceptor Thus, the two substrates of this enzyme are D-sorbitol and acceptor, whereas its two products are L-sorbose and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-sorbitol:acceptor 1-oxidoreductase. This enzyme is also called D-sorbitol:(acceptor) 1-oxidoreductase.

Uracil/thymine dehydrogenase (, uracil oxidase, uracil-thymine oxidase, uracil dehydrogenase) is an enzyme with systematic name uracil:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : (1) uracil + H2O + acceptor \rightleftharpoons barbiturate + reduced acceptor : (2) thymine + H2O + acceptor \rightleftharpoons 5-methylbarbiturate + reduced acceptor Uracil/thymine dehydrogenase forms part of the oxidative pyrimidine- degrading pathway in some microorganisms.

In enzymology, a tetrachloroethene reductive dehalogenase () is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family. :trichloroethene + chloride + acceptor \rightleftharpoons tetrachloroethene + reduced acceptor The 3 substrates of this enzyme are trichloroethene, chloride, and acceptor, whereas its two products are tetrachloroethene and reduced acceptor. This enzyme belongs to the family of oxidoreductases.

Uracil dehydrogenase (, uracil oxidase) is an enzyme with systematic name uracil:(acceptor) oxidoreductase. This enzyme catalyses the following chemical reaction : uracil + acceptor \rightleftharpoons barbiturate + reduced acceptor Also oxidizes thymine. The enzyme acts on the hydrated derivative of the substrate.

Arsenate reductase (donor) () is an enzyme that catalyzes the chemical reaction :arsenite + acceptor \rightleftharpoons arsenate + reduced acceptor Thus, the two substrates of this enzyme are arsenite and an acceptor, whereas its two products are arsenate and a reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with other acceptors. The systematic name of this enzyme class is arsenate:acceptor oxidoreductase. This enzyme is also called arsenate:(acceptor) oxidoreductase.

In enzymology, an alcohol dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :a primary alcohol + acceptor \rightleftharpoons an aldehyde + reduced acceptor Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase.

In enzymology, a fructose 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction :D-fructose + acceptor \rightleftharpoons 5-dehydro-D- fructose + reduced acceptor Thus, the two substrates of this enzyme are D-fructose and acceptor, whereas its two products are 5-dehydro-D-fructose and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-fructose:acceptor 5-oxidoreductase. Other names in common use include fructose 5-dehydrogenase (acceptor), D-fructose dehydrogenase, and D-fructose:(acceptor) 5-oxidoreductase.

In enzymology, a glucose dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :D-glucose + acceptor \rightleftharpoons D-glucono-1,5-lactone + reduced acceptor Thus, the two substrates of this enzyme are D-glucose and acceptor, whereas its two products are D-glucono-1,5-lactone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-glucose:acceptor 1-oxidoreductase. Other names in common use include glucose dehydrogenase (Aspergillus), glucose dehydrogenase (decarboxylating), and D-glucose:(acceptor) 1-oxidoreductase.

In enzymology, a 4-hydroxybenzoyl-CoA reductase () is an enzyme found in some bacteria and archaea that catalyzes the chemical reaction :benzoyl-CoA + acceptor + H2O \rightleftharpoons 4-hydroxybenzoyl-CoA + reduced acceptor The 3 substrates of this enzyme are benzoyl-CoA, acceptor, and H2O, whereas its two products are 4-hydroxybenzoyl-CoA and reduced acceptor. This enzyme participates in benzoate degradation via coa ligation.

In enzymology, a D-2-hydroxyglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(R)-2-hydroxyglutarate + acceptor \rightleftharpoons 2-oxoglutarate + reduced acceptor Thus, the two substrates of this enzyme are (R)-2-hydroxyglutarate and acceptor, whereas its two products are 2-oxoglutarate and reduced acceptor. The enzyme activity has been confirmed in animals as well as in plants .

This mutation is in a splice acceptor site of exon 3. The loss of this acceptor site reveals a downstream cryptic acceptor site and a protein missing 5 amino acids in the N-terminus (I70_E74del). This mutation has not been further characterized.

Known mechanisms include Kerberos, NTLM, Distributed Computing Environment (DCE), SESAME, SPKM, LIPKEY. ;Initiator/acceptor :The peer that sends the first token is the initiator; the other is the acceptor. Generally, the client program is the initiator while the server is the acceptor.

In enzymology, a carboxylate reductase () is an enzyme that catalyzes the chemical reaction :an aldehyde + acceptor + H2O \rightleftharpoons a carboxylate + reduced acceptor The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase. This enzyme is also called aldehyde:(acceptor) oxidoreductase.

In enzymology, a taurine dehydrogenase () is an enzyme that catalyzes the chemical reaction :taurine + H2O + acceptor \rightleftharpoons sulfoacetaldehyde + NH3 \+ reduced acceptor The 3 substrates of this enzyme are taurine, H2O, and acceptor, whereas its 3 products are sulfoacetaldehyde, NH3, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other acceptors. The systematic name of this enzyme class is taurine:acceptor oxidoreductase (deaminating). This enzyme is also called taurine:(acceptor) oxidoreductase (deaminating).

Modified chlorophyll a0 is an early electron acceptor in PSI. Chlorophyll a0 accepts electrons from P700 before passing them along to another early electron acceptor.

In both types of bonding, an electron donor/electron acceptor relationship exists. The difference between the two is what species can act as the electron donor/electron acceptor. In hydrogen bonding, a hydrogen atom acts as the electron acceptor and forms a non- covalent interaction by accepting electron density from an electron rich site (electron donor). In halogen bonding, a halogen atom is the electron acceptor.

Finally, glycosythase are specific for the donor sugar but often have loose specificity for the acceptor sugar. This can result in different regioselectivity depending on the acceptor resulting in products with different glycosidic linkages. One example is the Agrobacterium sp. β-glucosythase, which forms a β 1-4 glycoside with Glucose as the acceptor, but forms a β 1-3 glycoside with Xylose as the acceptor.

An AFA is the set of all acceptors over a given pair of state and input alphabets which have the same storage mechanism defined by a given AFA schema. The \vdash relation defines one step in the operation of an acceptor. L_f(D) is the set of words accepted by acceptor D by having the acceptor enter an accepting state. L(D) is the set of words accepted by acceptor D by having the acceptor simultaneously enter an accepting state and having an empty storage.

In enzymology, a cyclohexanone dehydrogenase () is an enzyme that catalyzes a chemical reaction :cyclohexanone + acceptor \rightleftharpoons cyclohex-2-enone + reduced acceptor Thus, the two substrates of this enzyme are cyclohexanone and acceptor, whereas its two products are cyclohex-2-enone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:(acceptor) 2-oxidoreductase.

In enzymology, a glycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction :glycolate + acceptor \rightleftharpoons glyoxylate + reduced acceptor Thus, the two substrates of this enzyme are glycolate and acceptor, whereas its two products are glyoxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is glycolate:acceptor 2-oxidoreductase. Other names in common use include glycolate oxidoreductase, glycolic acid dehydrogenase, and glycolate:(acceptor) 2-oxidoreductase.

In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) () is an enzyme that catalyzes the chemical reaction :an aldehyde + acceptor + H2O \rightleftharpoons a carboxylate + reduced acceptor The 3 substrates of this enzyme are aldehyde, acceptor, and H2O, whereas its two products are carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called aldehyde dehydrogenase (acceptor).

In enzymology, an ethylbenzene hydroxylase () is an enzyme that catalyzes the chemical reaction :ethylbenzene + H2O + acceptor \rightleftharpoons (S)-1-phenylethanol + reduced acceptor The 3 substrates of this enzyme are ethylbenzene, H2O, and acceptor, whereas its two products are (S)-1-phenylethanol and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is ethylbenzene:acceptor oxidoreductase. Other names in common use include ethylbenzene dehydrogenase, and ethylbenzene:(acceptor) oxidoreductase.

In enzymology, a spermidine dehydrogenase () is an enzyme that catalyzes the chemical reaction :spermidine + acceptor + H2O \rightleftharpoons propane-1,3-diamine + 4-aminobutanal + reduced acceptor The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase.

In enzymology, a cellobiose dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :cellobiose + acceptor \rightleftharpoons cellobiono-1,5-lactone + reduced acceptor Thus, the two substrates of this enzyme are cellobiose and acceptor, whereas its two products are cellobiono-1,5-lactone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is cellobiose:acceptor 1-oxidoreductase. Other names in common use include cellobiose dehydrogenase, cellobiose oxidoreductase, Phanerochaete chrysosporium cellobiose oxidoreductase, CBOR, cellobiose oxidase, cellobiose:oxygen 1-oxidoreductase, CDH, and cellobiose:(acceptor) 1-oxidoreductase.

Pyranose dehydrogenase (acceptor) (, pyranose dehydrogenase, pyranose-quinone oxidoreductase, quinone-dependent pyranose dehydrogenase, PDH) is an enzyme with systematic name pyranose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : (1) a pyranose + acceptor \rightleftharpoons a pyranos-2-ulose (or a pyranos-3-ulose or a pyranos-2,3-diulose) + reduced acceptor : (2) a pyranoside + acceptor \rightleftharpoons a pyranosid-3-ulose (or a pyranosid-3,4-diulose) + reduced acceptor This enzyme requires FAD. A number of aldoses and ketoses in pyranose form, as well as glycosides, gluco- oligosaccharides, sucrose and lactose can act as a donor.

In enzymology, a 4-cresol dehydrogenase (hydroxylating) () is an enzyme that catalyzes the chemical reaction :4-cresol + acceptor + H2O \rightleftharpoons 4-hydroxybenzaldehyde + reduced acceptor The 3 substrates of this enzyme are 4-cresol, acceptor, and H2O, whereas its two products are 4-hydroxybenzaldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is 4-cresol:acceptor oxidoreductase (methyl-hydroxylating). Other names in common use include p-cresol–(acceptor) oxidoreductase (hydroxylating), and p-cresol methylhydroxylase.

In enzymology, a NADPH dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction :NADPH + H+ \+ acceptor \rightleftharpoons NADP+ \+ reduced acceptor The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide phosphate (quinone), dehydrogenase, NADPH oxidase, and NADPH2 dehydrogenase (quinone).

In enzymology, a L-pipecolate dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-pipecolate + acceptor \rightleftharpoons 2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor Thus, the two substrates of this enzyme are L-pipecolate and acceptor, whereas its two products are 2,3,4,5-tetrahydropyridine-2-carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is L-pipecolate:acceptor 1,6-oxidoreductase. This enzyme is also called L-pipecolate:(acceptor) 1,6-oxidoreductase.

A glycosyl acceptor is any suitable nucleophile-containing molecule that will react with a glycosyl donor to form a new glycosidic bond. By convention, the acceptor is the member of this pair which did not contain the resulting anomeric carbon of the new glycosidic bond. Since the nucleophilic atom of the acceptor is typically an oxygen atom, this can be remembered using the mnemonic of the acceptor is the alcohol. A glycosyl acceptor can be a mono- or oligosaccharide that contains an available nucleophile, such as an unprotected hydroxyl.

In enzymology, a sorbose dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-sorbose + acceptor \rightleftharpoons 5-dehydro-D- fructose + reduced acceptor Thus, the two substrates of this enzyme are L-sorbose and acceptor, whereas its two products are 5-dehydro-D-fructose and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is L-sorbose:acceptor 5-oxidoreductase. This enzyme is also called L-sorbose:(acceptor) 5-oxidoreductase.

In enzymology, a glucoside 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction :sucrose + acceptor \rightleftharpoons 3-dehydro-alpha-D- glucosyl-beta-D-fructofuranoside + reduced acceptor Thus, the two substrates of this enzyme are sucrose and acceptor, whereas its two products are 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside and reduced acceptor. This enzyme participates in galactose metabolism and starch and sucrose metabolism. It employs one cofactor, FAD.

In enzymology, an agaritine gamma-glutamyltransferase () is an enzyme that catalyzes the chemical reaction :agaritine + acceptor \rightleftharpoons 4-hydroxymethylphenylhydrazine + gamma-L-glutamyl-acceptor Thus, the two substrates of this enzyme are agaritine and acceptor, whereas its two products are 4-hydroxymethylphenylhydrazine and gamma-L-glutamyl-acceptor. This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is (gamma-L- glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:acceptor gamma- glutamyltransferase. Other names in common use include (gamma-L- glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:(acceptor), gamma- glutamyltransferase, (gamma-L- glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:(acceptor), gamma- glutamyltransferase, (gamma-L- glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:acceptor, and gamma- glutamyltransferase.

In enzymology, a gluconate 2-dehydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :D-gluconate + acceptor \rightleftharpoons 2-dehydro-D-gluconate + reduced acceptor Thus, the two substrates of this enzyme are D-gluconate and acceptor, whereas its two products are 2-dehydro-D- gluconate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-gluconate:acceptor 2-oxidoreductase. Other names in common use include gluconate oxidase, gluconate dehydrogenase, gluconic dehydrogenase, D-gluconate dehydrogenase, gluconic acid dehydrogenase, 2-ketogluconate reductase, D-gluconate dehydrogenase, 2-keto-D-gluconate-yielding, and D-gluconate:(acceptor) 2-oxidoreductase.

In enzymology, a formylmethanofuran dehydrogenase () is an enzyme that catalyzes the chemical reaction: :formylmethanofuran + H2O + acceptor \rightleftharpoons CO2 \+ methanofuran + reduced acceptor. The 3 substrates of this enzyme are formylmethanofuran, H2O, and acceptor, whereas its 3 products are CO2, methanofuran, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is formylmethanofuran:acceptor oxidoreductase.

Formate dehydrogenase (acceptor) (, FDHH, FDH-H, FDH-O, formate dehydrogenase H, formate dehydrogenase O) is an enzyme with systematic name formate:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : formate + acceptor \rightleftharpoons CO2 \+ reduced acceptor Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer] transferring electrons to a hydrogenase.

Beta-cyclopiazonate dehydrogenase () is an enzyme that catalyzes the chemical reaction 600px :beta-cyclopiazonate + acceptor \rightleftharpoons alpha- cyclopiazonate + reduced acceptor Thus, the two substrates of this enzyme are beta-cyclopiazonate and an acceptor, whereas its two products are alpha- cyclopiazonate and a reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with other acceptors. The systematic name of this enzyme class is beta- cyclopiazonate:acceptor oxidoreductase (cyclizing). Other names in common use include beta-cyclopiazonate oxidocyclase, beta-cyclopiazonic oxidocyclase, and beta-cyclopiazonate:(acceptor) oxidoreductase (cyclizing).

In enzymology, a hydrogensulfite reductase () is an enzyme that catalyzes the chemical reaction :trithionate + acceptor + 2 H2O + OH- \rightleftharpoons 3 bisulfite + reduced acceptor The 4 substrates of this enzyme are trithionate, acceptor, H2O, and OH-, whereas its two products are bisulfite and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is trithionate:acceptor oxidoreductase. Other names in common use include bisulfite reductase, dissimilatory sulfite reductase, desulfoviridin, desulforubidin, desulfofuscidin, dissimilatory-type sulfite reductase, and trithionate:(acceptor) oxidoreductase.

In enzymology, a dimethylglycine dehydrogenase () is an enzyme that catalyzes the chemical reaction :N,N-dimethylglycine + acceptor + H2O \rightleftharpoons sarcosine + formaldehyde + reduced acceptor The 3 substrates of this enzyme are N,N-dimethylglycine, acceptor, and H2O, whereas its 3 products are sarcosine, formaldehyde, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N,N-dimethylglycine:acceptor oxidoreductase (demethylating). Other names in common use include N,N-dimethylglycine oxidase, and N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating).

Adenylyl-sulfate reductase () is an enzyme that catalyzes the chemical reaction :AMP + sulfite + acceptor \rightleftharpoons adenylyl sulfate + reduced acceptor The 3 substrates of this enzyme are AMP, sulfite, and an acceptor, whereas its two products are adenylyl sulfate and a reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming). Other names in common use include adenosine phosphosulfate reductase, adenosine 5'-phosphosulfate reductase, APS-reductase, APS reductase, AMP, sulfite:(acceptor) oxidoreductase, and (adenosine-5'-phosphosulfate-forming).

In enzymology, a pyridoxine 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction :pyridoxine + acceptor \rightleftharpoons isopyridoxal + reduced acceptor Thus, the two substrates of this enzyme are pyridoxine and acceptor, whereas its two products are isopyridoxal and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is pyridoxine:acceptor 5-oxidoreductase. Other names in common use include pyridoxal-5-dehydrogenase, pyridoxol 5-dehydrogenase, pyridoxin 5-dehydrogenase, pyridoxine dehydrogenase, pyridoxine 5'-dehydrogenase, and pyridoxine:(acceptor) 5-oxidoreductase.

In enzymology, a D-2-hydroxy-acid dehydrogenase () is an enzyme that catalyzes the chemical reaction :(R)-lactate + acceptor \rightleftharpoons pyruvate + reduced acceptor Thus, the two substrates of this enzyme are (R)-lactate and acceptor, whereas its two products are pyruvate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. Other names in common use include D-2-hydroxy acid dehydrogenase, and (R)-2-hydroxy- acid:(acceptor) 2-oxidoreductase.

In enzymology, a nicotine dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-nicotine + acceptor + H2O \rightleftharpoons (S)-6-hydroxynicotine + reduced acceptor The 3 substrates of this enzyme are (S)-nicotine, acceptor, and H2O, whereas its two products are (S)-6-hydroxynicotine and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is nicotine:acceptor 6-oxidoreductase (hydroxylating). Other names in common use include nicotine oxidase, D-nicotine oxidase, nicotine:(acceptor) 6-oxidoreductase (hydroxylating), and L-nicotine oxidase.

In enzymology, a methylglutamate dehydrogenase () is an enzyme that catalyzes the chemical reaction :N-methyl-L-glutamate + acceptor + H2O \rightleftharpoons L-glutamate + formaldehyde + reduced acceptor The 3 substrates of this enzyme are N-methyl-L-glutamate, acceptor, and H2O, whereas its 3 products are L-glutamate, formaldehyde, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N-methyl-L-glutamate:acceptor oxidoreductase (demethylating). Other names in common use include N-methylglutamate dehydrogenase, and N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating).

During the process an intramolecular trisulfide is formed between two L-cysteine residues of DsrC and the sulfur atom from sulfite. This trisulfide can be reduced by a number of proteins including DsrK and TcmB. Reaction in organisms performing dissimilatory sulfate reduction: : (1) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O (overall reaction) :: (1a) sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = a [DsrC protein]-S-sulfanyl-L-cysteine + 2 acceptor + 3 H2O :: (1b) a [DsrC protein]-S-sulfanyl-L-cysteine = hydrogen sulfide + a [DsrC protein]-disulfide Reaction in organisms performing sulfur oxidation: : (2) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+ (overall reaction) :: (2a) a [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = a [DsrC]-S-sulfo-L-cysteine + 3 reduced acceptor + H+ :: (2b) a [DsrC]-S-sulfo-L-cysteine = sulfite + a [DsrC protein]-disulfide The systematic name of this enzyme class is hydrogen-sulfide:[DsrC sulfur-carrier protein],acceptor oxidoreductase. This enzyme is different from EC 1.8.

O-aminophenol oxidase (, isophenoxazine synthase, o-aminophenol:O2 oxidoreductase, 2-aminophenol:O2 oxidoreductase, GriF) is an enzyme with systematic name 2-aminophenol:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction : 2 2-aminophenol + O2 \+ acceptor \rightleftharpoons 2-aminophenoxazin-3-one + reduced acceptor + 2 H2O (overall reaction) : (1a) 2 2-aminophenol + O2 \rightleftharpoons 2 6-iminocyclohexa-2,4-dienone + 2 H2O : (1b) 2 6-iminocyclohexa-2,4-dienone + acceptor \rightleftharpoons 2-aminophenoxazin-3-one + reduced acceptor (spontaneous) O-aminophenol oxidase is a flavoprotein.

In enzymology, a 3-hydroxycyclohexanone dehydrogenase () is an enzyme that catalyzes the chemical reaction :3-hydroxycyclohexanone + acceptor \rightleftharpoons cyclohexane-1,3-dione + reduced acceptor Thus, the two substrates of this enzyme are 3-hydroxycyclohexanone and acceptor, whereas its two products are cyclohexane-1,3-dione and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with other acceptors. The systematic name of this enzyme class is 3-hydroxycyclohexanone:acceptor 1-oxidoreductase.

Jablonski diagram of FRET Fluorescence Resonance Energy Transfer (FRET) utilizes energy transferred between the donor and the acceptor molecules that are in close proximity. FRET uses a fluorescently labeled ligand, as with FP. Energy transfer within FRET begins by exciting the donor. The dipole-dipole interaction between the donor and the acceptor molecule transfers the energy from the donor to the acceptor molecule. If the ligand is bound to the receptor-antibody complex, then the acceptor will emit light.

Three different schematic representations of blending electron donor and acceptor materials. (a) Bilayer representation, with efficient charge generation but poor charge transport.[10] (b) Solution processed representation, in which rapid drying leads to a randomized network of acceptor/donor blending, currently the most optimal way to blend. (c) Theoretical, ideal representation of acceptor/donor blending.

Soluble quinoprotein glucose dehydrogenase (, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with systematic name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : D-glucose + acceptor \rightleftharpoons D-glucono-1,5-lactone + reduced acceptor This soluble periplasmic enzyme contains PQQ as prosthetic group, and is bound to a calcium ion. Electron acceptor is not known.

An acceptor could also be described as defining a language that would contain every string accepted by the acceptor but none of the rejected ones; that language is accepted by the acceptor. By definition, the languages accepted by acceptors are the regular languages. The problem of determining the language accepted by a given acceptor is an instance of the algebraic path problem—itself a generalization of the shortest path problem to graphs with edges weighted by the elements of an (arbitrary) semiring., p.

In enzymology, an isoquinoline 1-oxidoreductase () is an enzyme that catalyzes the chemical reaction :isoquinoline + acceptor + H2O \rightleftharpoons isoquinolin-1(2H)-one + reduced acceptor The 3 substrates of this enzyme are isoquinoline, acceptor, and H2O, whereas its two products are isoquinolin-1(2H)-one and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is isoquinoline:acceptor 1-oxidoreductase (hydroxylating).

In enzymology, a quinoline 2-oxidoreductase () is an enzyme that catalyzes the chemical reaction :quinoline + acceptor + H2O \rightleftharpoons quinolin-1(2H)-one + reduced acceptor The 3 substrates of this enzyme are quinoline, acceptor, and H2O, whereas its two products are quinolin-1(2H)-one and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline:acceptor 2-oxidoreductase (hydroxylating).

In enzymology, an isovaleryl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :3-methylbutanoyl-CoA + acceptor \rightleftharpoons 3-methylbut-2-enoyl-CoA + reduced acceptor Thus, the two substrates of this enzyme are 3-methylbutanoyl-CoA and acceptor, whereas its two products are 3-methylbut-2-enoyl-CoA and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase.

In enzymology, a 2-methylacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :2-methylbutanoyl-CoA + acceptor \rightleftharpoons 2-methylbut-2-enoyl-CoA + reduced acceptor Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and acceptor, whereas its two products are 2-methylbut-2-enoyl-CoA and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include branched-chain acyl-CoA dehydrogenase, 2-methyl branched chain acyl- CoA dehydrogenase, and 2-methylbutanoyl-CoA:(acceptor) oxidoreductase.

In enzymology, a 3-oxo-5beta-steroid 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction :a 3-oxo-5beta-steroid + acceptor \rightleftharpoons a 3-oxo-Delta4-steroid + reduced acceptor Thus, the two substrates of this enzyme are 3-oxo-5beta-steroid and acceptor, whereas its two products are 3-oxo-Delta4-steroid and reduced acceptor. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxo-5beta-steroid:acceptor Delta4-oxidoreductase. This enzyme is also called 3-oxo-5beta-steroid:(acceptor) Delta4-oxidoreductase.

There are a few distinct mechanisms by which energy can be transferred non-radiatively (without absorption or emission of photons) between two dyes, a donor and an acceptor. Förster resonance energy transfer (FRET or FET) is a dynamic quenching mechanism because energy transfer occurs while the donor is in the excited state. FRET is based on classical dipole-dipole interactions between the transition dipoles of the donor and acceptor and is extremely dependent on the donor- acceptor distance, R, falling off at a rate of 1/R6. FRET also depends on the donor-acceptor spectral overlap (see figure) and the relative orientation of the donor and acceptor transition dipole moments.

In enzymology, a 3-oxosteroid 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction :a 3-oxosteroid + acceptor \rightleftharpoons a 3-oxo- Delta1-steroid + reduced acceptor Thus, the two substrates of this enzyme are 3-oxosteroid and acceptor, whereas its two products are 3-oxo-Delta1-steroid and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxosteroid:acceptor Delta1-oxidoreductase. Other names in common use include 3-oxosteroid Delta1-dehydrogenase, Delta1-dehydrogenase, 3-ketosteroid-1-en-dehydrogenase, 3-ketosteroid-Delta1-dehydrogenase, 1-ene-dehydrogenase, 3-oxosteroid:(2,6-dichlorphenolindophenol) Delta1-oxidoreductase, 4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase, Delta1-steroid reductase, and 3-oxosteroid:(acceptor) Delta1-oxidoreductase.

In superacids, the proton is shuttled rapidly from proton acceptor to proton acceptor by tunneling through a hydrogen bond via the Grotthuss mechanism, just as in other hydrogen-bonded networks, like water or ammonia.

In enzymology, a quinaldate 4-oxidoreductase () is an enzyme that catalyzes the chemical reaction :quinaldate + acceptor + H2O \rightleftharpoons kynurenate + reduced acceptor The 3 substrates of this enzyme are quinaldate, acceptor, and H2O, whereas its two products are kynurenate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating). This enzyme is also called quinaldic acid 4-oxidoreductase.

Note that oxidases typically transfer the equivalent of dihydrogen (H2), and the acceptor is a dioxygen. Similarly, a peroxidase (another subclass of oxidoreductases) will use a peroxide (H2O2) as the electron acceptor, rather than an oxygen.

In enzymology, a 2-furoyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :2-furoyl-CoA + H2O + acceptor \rightleftharpoons S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor The 3 substrates of this enzyme are 2-furoyl-CoA, H2O, and acceptor, whereas its two products are S-(5-hydroxy-2-furoyl)-CoA and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating). Other names in common use include furoyl-CoA hydroxylase, 2-furoyl coenzyme A hydroxylase, 2-furoyl coenzyme A dehydrogenase, and 2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating).

In enzymology, a cytokinin dehydrogenase () is an enzyme that catalyzes the chemical reaction :N6-dimethylallyladenine + electron acceptor + H2O \rightleftharpoons adenine + 3-methylbut-2-enal + reduced acceptor The 3 substrates of this enzyme are cytokinin (here represented by N6-dimethylallyladenine), electron acceptor, and H2O, whereas its 3 products are adenine, 3-methylbut-2-enal (or other aldehyde in case of different substrate), and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is N6-dimethylallyladenine:acceptor oxidoreductase. Other names in common use include N6-dimethylallyladenine:(acceptor) oxidoreductase, 6-N-dimethylallyladenine:acceptor oxidoreductase, and cytokinin oxidase/dehydrogenase abbreviated as CKX.

In enzymology, a NADPH dehydrogenase () is an enzyme that catalyzes the chemical reaction :NADPH + H+ \+ acceptor \rightleftharpoons NADP+ \+ reduced acceptor The 3 substrates of this enzyme are NADPH, H+, and acceptor, whereas its two products are NADP+ and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADPH:acceptor oxidoreductase. Other names in common use include NADPH2 diaphorase, NADPH diaphorase, OYE, diaphorase, dihydronicotinamide adenine dinucleotide phosphate dehydrogenase, NADPH-dehydrogenase, NADPH-diaphorase, NADPH2-dehydrogenase, old yellow enzyme, reduced nicotinamide adenine dinucleotide phosphate dehydrogenase, TPNH dehydrogenase, TPNH-diaphorase, triphosphopyridine diaphorase, triphosphopyridine nucleotide diaphorase, NADPH2 dehydrogenase, and NADPH:(acceptor) oxidoreductase.

With antimony pentafluoride, SbF5, a fluoride acceptor, the ReF6+ cation is formed.

In enzymology, an aldehyde dehydrogenase (FAD-independent) () is an enzyme that catalyzes the chemical reaction :an aldehyde + H2O + acceptor \rightleftharpoons a carboxylate + reduced acceptor The 3 substrates of this enzyme are aldehyde, H2O, and acceptor, whereas its two products are carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase (FAD-independent). Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd.

Hydrazine oxidoreductase (, HAO (ambiguous)) is an enzyme with systematic name hydrazine:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : hydrazine + acceptor \rightleftharpoons N2 \+ reduced acceptor Hydrazine oxidoreductase is involved in the pathway of anaerobic ammonium oxidation in anammox bacteria.

Similar to the graded heterojunction the continuous junction concept aims at realizing a gradual transition from an electron donor to an electron acceptor. However, the acceptor material is prepared directly from the donor polymer in a post- polymerization modification step.

Charge-transfer occurs from the polymer to the acceptor compound; the polyacetylene chain acts as a cation and the acceptor as an anion. The “hole” on the polymer backbone is weakly associated with the anionic acceptor by Coulomb potential. Polyacetylene doped with (p-type) dopants retain their high conductivity even after exposure to air for several days. Electron-donating (n-type) dopants can also be used to create conductive polyacetylene.

The distinction between the subclasses of oxidoreductases that catalyze oxidation reactions lies in their electron acceptors. Reaction catalyzed by an oxidase, note the reduction of oxygen as the electron acceptor Dehydrogenase and oxidase are easily distinguishable if one considers the electron acceptor. An oxidase will remove electrons from a substrate as well, but only uses oxygen as its electron acceptor. One such reaction is: AH2 \+ O2 ↔ A + H2O2.

In nature, denitrification can take place in both terrestrial and marine ecosystems. Typically, denitrification occurs in anoxic environments, where the concentration of dissolved and freely available oxygen is depleted. In these areas, nitrate (NO3−) or nitrite (−) can be used as a substitute terminal electron acceptor instead of oxygen (O2), a more energetically favourable electron acceptor. Terminal electron acceptor is a compound that gets reduced in the reaction by receiving electrons.

All of the members in this family use acyl-CoA as the acceptor molecule.

Faraday Soc., 1969,65, 41-51 HNCS acceptor properties are discussed in the ECW model.

Cells that use molecular oxygen (O2) as their final electron acceptor are described as using aerobic respiration, while cells that use other soluble compounds as their final electron acceptor are described as using anaerobic respiration. However, the final electron acceptor of an exoelectrogen is found extracellularly and can be a strong oxidizing agent in aqueous solution or a solid conductor/electron acceptor. Two commonly observed acceptors are iron compounds (specifically Fe(III) oxides) and manganese compounds (specifically Mn(III/IV) oxides). As oxygen is a strong oxidizer, cells are able to do this strictly in the absence of oxygen.

In enzymology, a (R)-pantolactone dehydrogenase (flavin) () is an enzyme that catalyzes the chemical reaction :(R)-pantolactone + acceptor \rightleftharpoons 2-dehydropantolactone + reduced acceptor Thus, the two substrates of this enzyme are (R)-pantolactone and acceptor, whereas its two products are 2-dehydropantolactone and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (R)-pantolactone:acceptor oxidoreductase (flavin-containing). Other names in common use include 2-dehydropantolactone reductase (flavin), 2-dehydropantoyl- lactone reductase (flavin), and (R)-pantoyllactone dehydrogenase (flavin).

In enzymology, a 2-oxo-acid reductase () is an enzyme that catalyzes the chemical reaction :a (2R)-hydroxy-carboxylate + acceptor \rightleftharpoons a 2-oxo-carboxylate + reduced acceptor Thus, the two substrates of this enzyme are (2R)-hydroxy-carboxylate and acceptor, whereas its two products are 2-oxo- carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (2R)-hydroxy- carboxylate:acceptor oxidoreductase. Other names in common use include (2R)-hydroxycarboxylate-viologen-oxidoreductase, HVOR, and 2-oxoacid reductase.

The generalized electron transport chain in bacteria is: Donor Donor Donor ↓ ↓ ↓ dehydrogenase → quinone → bc1 → cytochrome ↓ ↓ oxidase(reductase) oxidase(reductase) ↓ ↓ Acceptor Acceptor Electrons can enter the chain at three levels: at the level of a dehydrogenase, at the level of the quinone pool, or at the level of a mobile cytochrome electron carrier. These levels correspond to successively more positive redox potentials, or to successively decreased potential differences relative to the terminal electron acceptor. In other words, they correspond to successively smaller Gibbs free energy changes for the overall redox reaction Donor → Acceptor. Individual bacteria use multiple electron transport chains, often simultaneously.

Alcohol dehydrogenase (nicotinoprotein) (, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : ethanol + acceptor \rightleftharpoons acetaldehyde + reduced acceptor This enzyme contains Zn2+.

Methanol dehydrogenase (nicotinoprotein) (, NDMA-dependent methanol dehydrogenase, nicotinoprotein methanol dehydrogenase, methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : methanol + acceptor \rightleftharpoons formaldehyde + reduced acceptor This enzyme contains Zn2+ and Mg2+.

Furthermore, the ligand functions as a proton acceptor thus eliminating the need of a base.

Fig. 4: Acceptor FSM: parsing the string "nice". Fig. 5: Representation of an acceptor; this example shows one that determines whether a binary number has an even number of 0s, where S1 is an accepting state and S2 is a non accepting state. Acceptors (also called detectors or recognizers) produce binary output, indicating whether or not the received input is accepted. Each state of an acceptor is either accepting or non accepting.

Different protecting groups on either the glycosyl donor or the glycosyl acceptor may affect the reactivity and yield of the glycosylation reaction. Typically, electron-withdrawing groups such as acetyl or benzoyl groups are found to decrease the reactivity of the donor/acceptor and are therefore termed "disarming" groups. Electron-donating groups such as the benzyl group, are found to increase the reactivity of the donor/acceptor and are therefore called "arming" groups.

In reaction two, after acetyl-CoA is released, the acetyl acceptor interacts with the acetylated enzyme to form product. This second reaction is independent of the acetyl donor since it leaves the enzyme before the acetyl acceptor binds. However, like with many ping pong bi bi reactions, its possible there is competition between the acetyl donor and acetyl acceptor for the unacetylated enzyme. This leads to substrate-dependent inhibition at high concentrations.

Structure of the complex formed upon co- crystallization of pyromellitic anhydride (molecules terminated in red) and anthracene. PMDA is an electron-acceptor, forming a variety of charge-transfer complexes. It reacts with amines to diimides, C6H2[(CO)2NR]2 which also have acceptor properties.

This acceptor will finish in an accept state, if the binary string contains an even number of 0s (including any binary string containing no 0s). Examples of strings accepted by this acceptor are ε (the empty string), 1, 11, 11..., 00, 010, 1010, 10110, etc.

When using FRET, it is critical that there is a distance smaller than 10 nm between the acceptor and donor, in addition to an overlapping absorption spectrum between acceptor and donor, and that the antibody does not interfere or block the ligand binding site.

By connecting to other cells above them, nanowires allow bacteria located in anoxic conditions to still use oxygen as their terminal electron acceptor. For example, organisms in the genus Shewanella have been observed to form electrically conductive nanowires in response to electron-acceptor limitation.

It is a dienophile and a good Michael acceptor. Grignard reagents add to the carbonyl center.

In enzymology, a quinoline-4-carboxylate 2-oxidoreductase () is an enzyme that catalyzes the chemical reaction :quinoline-4-carboxylate + acceptor + H2O \rightleftharpoons 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor The 3 substrates of this enzyme are quinoline-4-carboxylate, acceptor, and H2O, whereas its two products are 2-oxo-1,2-dihydroquinoline-4-carboxylate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating). Other names in common use include quinaldic acid 4-oxidoreductase, and quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating).

In enzymology, a benzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction :benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O \rightleftharpoons cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate The 4 substrates of this enzyme are benzoyl-CoA, reduced acceptor, ATP, and H2O, whereas its 4 products are cyclohexa-1,5-diene-1-carbonyl-CoA, acceptor, ADP, and phosphate. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP- forming). This enzyme is also called benzoyl-CoA reductase (dearomatizing).

In enzymology, an L-2-hydroxyglutarate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-2-hydroxyglutarate + acceptor \rightleftharpoons 2-oxoglutarate + reduced acceptor Thus, the two substrates of this enzyme are (S)-2-hydroxyglutarate and acceptor, whereas its two products are 2-oxoglutarate and reduced acceptor. Enzymes which preferentially catalyze the conversion of the (R) stereoisomer of 2-oxoglutarate also exist in both mammals and plants and are named D-2-hydroxyglutarate dehydrogenase. L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; L-2-hydroxyglutarate dehydrogenase is an example of a metabolite repair enzyme that oxidizes L-2-hydroxyglutarate back to 2-oxoglutarate.

In enzymology, a dehydrogluconate dehydrogenase () is an enzyme that catalyzes the chemical reaction :2-dehydro-D-gluconate + acceptor \rightleftharpoons 2,5-didehydro-D-gluconate + reduced acceptor Thus, the two substrates of this enzyme are 2-dehydro-D-gluconate and acceptor, whereas its two products are 2,5-didehydro-D-gluconate and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is 2-dehydro-D-gluconate:acceptor 2-oxidoreductase. Other names in common use include ketogluconate dehydrogenase, alpha-ketogluconate dehydrogenase, 2-keto-D-gluconate dehydrogenase, and 2-oxogluconate dehydrogenase.

D-proline dehydrogenase (, D-Pro DH, D-Pro dehydrogenase, dye-linked D-proline dehydrogenase) is an enzyme with systematic name D-proline:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : D-proline + acceptor \rightleftharpoons 1-pyrroline-2-carboxylate + reduced acceptor This enzyme is a flavoprotein (FAD).

For instance, a write request on a file in a distributed file server. ; Acceptor (Voters): The Acceptors act as the fault-tolerant "memory" of the protocol. Acceptors are collected into groups called Quorums. Any message sent to an Acceptor must be sent to a Quorum of Acceptors.

Aralkylamine dehydrogenase (azurin) (, aromatic amine dehydrogenase, arylamine dehydrogenase, tyramine dehydrogenase) is an enzyme with the systematic name aralkylamine:azurin oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction: : ArCH2NH2 \+ H2O + 2 azurin \rightleftharpoons ArCHO + NH3 \+ 2 reduced azurin The three substrates of this enzyme are RCH2NH2 (i.e., an aromatic amine), water, and the acceptor azurin, and its three products are RCHO, ammonia, and a reduced acceptor. Azurin can be replaced with the artificial acceptor phenazine methosulfate in in vitro studies.

Excitation of the donor by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor if the two are within a given proximity to each other. The acceptor in turn emits light at its characteristic wavelength. The FRET aspect of the technology is driven by several factors, including spectral overlap and the proximity of the fluorophores involved, wherein energy transfer occurs only when the distance between the donor and the acceptor is small enough.

Glutaryl-CoA dehydrogenase (non-decarboxylating) (, GDHDes, nondecarboxylating glutaryl-coenzyme A dehydrogenase, nondecarboxylating glutaconyl-coenzyme A-forming GDH) is an enzyme with systematic name glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating). This enzyme catalyses the following chemical reaction : glutaryl-CoA + acceptor \rightleftharpoons (E)-glutaconyl- CoA + reduced acceptor The enzyme contains FAD.

In transhydrocyanation, an equivalent of HCN is transferred from a cyanohydrin, e.g. acetone cyanohydrin, to another HCN acceptor. The transfer is an equilibrium process, initiated by base. The reaction can be driven by trapping reactions or by the use of a superior HCN acceptor, such as an aldehyde.

Supramolecular chemistry was investigated, using donor and acceptor molecules that assemble upon spin casting and heating. Most supramolecular assemblies employ small molecules. Donor and acceptor domains in a tubular structure appear ideal for organic solar cells. Diblock polymers containing fullerene yield stable organic solar cells upon thermal annealing.

Normal circulation coins eventually collect microscopic particles of dirt, dust, oil and grease from people's fingers. When a coin acceptor is used for a long time, thousands of coins rolling along a track will leave enough dirt, dust, oil and grease to be visible. As a consequence of this, the coin acceptor must be cleaned properly on a regular basis to prevent malfunction or damage. Coin acceptors are modular, so a dirty acceptor can be replaced with a clean unit, minimising downtime.

This is caused by the P‑atom engaging in back bonding, as it is a π‑electron acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with a flavin as acceptor.

Other names in common use include assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase.

In enzymology, an all-trans-retinol 13,14-reductase () is an enzyme, encoded by the RETSAT gene, that catalyzes the chemical reaction :all- trans-13,14-dihydroretinol + acceptor \rightleftharpoons all-trans-retinol + reduced acceptor Thus, the two substrates of this enzyme are all- trans-13,14-dihydroretinol and acceptor, whereas its two products are all- trans-retinol and reduced acceptor. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of all-trans-retinol. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is all- trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is thiosulfate:ferricytochrome-c oxidoreductase. Other names in common use include tetrathionate synthase, thiosulfate oxidase, thiosulfate-oxidizing enzyme, and thiosulfate-acceptor oxidoreductase.

Electron current is inherent to the microbial metabolism. Microorganisms transfer electrons from an electron donor (lower potential species) to an electron acceptor (higher potential species). If the electron acceptor is an external ion or molecule, the process is called respiration. If the process is internal, electron transfer is called fermentation.

It has been prepared by oxidation of phenanthrene with chromic acid. It is used as a artificial mediator for electron acceptor/donor in Mo/W containing formate dehydrogenase reduction of Carbon dioxide to formate and vice versa. It is a better electron acceptor than the natural Nicodinamide adenosine dinucleotide(NAD+).

Tributylamine is used as a catalyst (proton acceptor) and as a solvent in organic syntheses and polymerization (including polyurethanes).

For singlet fragments, however, there is a double donor-acceptor bond with an angle of θ close to 45 °.

In fact, the electrical external quantum efficiency EQE_{EL} is highest for donor-acceptor blends with lowest driving force.

Alternative splicing of the Drosophila Transformer gene product. Pre-mRNAs of the Transformer (Tra) gene of Drosophila melanogaster undergo alternative splicing via the alternative acceptor site mode. The gene Tra encodes a protein that is expressed only in females. The primary transcript of this gene contains an intron with two possible acceptor sites.

Condition (3) insures the empty storage configuration is distinct from other configurations. Condition (4) requires there be an identity instruction that allows the state of memory to remain unchanged while the acceptor changes state or advances the input. Condition (5) assures that the set of storage symbols for any given acceptor is finite.

2-iminoacetate synthase (, thiH (gene)) is an enzyme with systematic name L-tyrosine 4-methylphenol-lyase (2-iminoacetate-forming). This enzyme catalyses the following chemical reaction : L-tyrosine + S-adenosyl-L- methionine + reduced acceptor \rightleftharpoons 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + acceptor + 2 H+ This enzyme binds a 4Fe-4S cluster.

Charge neutrality prevails in the field-free region because a negative acceptor ion creates a positive deficiency in the host material: a hole is the absence of an electron, it behaves like a positive charge. Where no field is present, neutrality is achieved because the negative acceptor ions exactly balance the positive holes.

The hydrates crystallize from aqueous hydrofluoric acid. The material is a fluoride acceptor. With xenon hexafluoride it forms [FeF4][XeF5].

For a two-dye system, the emission signals are then used to calculate the FRET efficiency between the dyes over time. The FRET efficiency is the number of photons emitted from the acceptor dye over the sum of the emissions of the donor and the acceptor dye. Usually, only the donor dye is excited, but even more accurate information can be obtained if donor and acceptor dye are alternatingly excited. In a single excitation scheme, the emission of the donor and acceptor dyes is just the number of photons collected for the two dyes divided by the photon collection efficiencies of the two channels respectively which are the functions of the collection efficiency, the filter and optical efficiency, and the camera efficiency of the two wavelength bands.

In molecular biology, proteins containing the carboxyl transferase domain include biotin-dependent carboxylases. This domain carries out the following reaction: transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxo acid as the acceptor molecule of carbon dioxide.

When the acceptor RuBP is in saturated concentration, gamma is independent of irradiation. However at low irradiation, only a small fraction of the sites on RuBP carboxylase-oxygenase (RuBisCO) have the electron acceptor RuBP. This decreases the photosynthetic activity and therefore affects gamma. The intracellular concentration of CO2 affects the rates of photosynthesis and photorespiration.

In the Ehb expression σacc and σdon are the screening charge densities of the hydrogen bond acceptor and donor respectively. The hydrogen bonding threshold σhb and the prefactor chb are adjustable parameters. The max[] and min[] construction ensures that the screening charge densities of the acceptor and donor exceeds the threshold for hydrogen bonding.

Excitation of the donor fluorophore (in this case, the lanthanide ion complex) by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor fluorophore if they are within a given proximity to each other (known as the Förster's radius). The acceptor fluorophore in turn emits light at its characteristic wavelength. The two most commonly used lanthanides in life science assays are shown below along with their corresponding acceptor dye as well as their excitation and emission wavelengths and resultant Stokes shift (separation of excitation and emission wavelengths).

The other material facilitates exciton dissociation at the junction. Charge is transferred and then separated after an exciton created in the donor is delocalized on a donor-acceptor complex. The acceptor material needs a suitable energy offset to the binding energy of the exciton to the absorber. Charge transfer is favorable if the following condition is satisfied: :E_A^A - E_A^D > U_D where superscripts A and D refer to the acceptor and donor respectively, EA is the electron affinity, and U the coulombic binding energy of the exciton on the donor.

Target compounds are extracted from an aqueous sample, through a µL-volume of organic solvent sustained as a thin supported liquid membrane (SLM) in the pores in the wall of a porous hollow fiber, and into an acceptor solution inside the lumen of the hollow fiber. Extraction is based on electrokinetic migration in an electrical field sustained across the SLM. The volume of the acceptor solution is typically 5-25 µL. The acceptor solution is an aqueous solution, and can be analyzed by liquid chromatography (LC) or capillary electrophoresis (CE).

Cellular respiration is the process by which biological fuels are oxidised in the presence of a high-energy inorganic electron acceptor (such as oxygen) to produce large amounts of energy, to drive the bulk production of ATP. Anaerobic respiration is used by some microorganisms in which neither oxygen (aerobic respiration) nor pyruvate derivatives (fermentation) is the high-energy final electron acceptor. Rather, an inorganic acceptor such as sulfate or nitrate is used. Such organisms are typically found in unusual places such as underwater caves or near hydrothermal vents at the bottom of the ocean.

This enzyme is also called formylmethanofuran:(acceptor) oxidoreductase. This enzyme participates in folate biosynthesis. It has 2 cofactors: molybdenum, and Pterin.

This processing is achieved when the outrons are trans-spliced to unpaired, downstream acceptor sites adjacent to cistron open reading frames.

There are two variants of the enzyme, one that uses NAD+ as a substrate, and one that uses NADP+ as acceptor.

It is a more practical choice for an electron acceptor when compared with fullerenes because of its solubility in chlorobenzene. This allows for solution processable donor/acceptor mixes, a necessary property for "printable" solar cells. However, considering the cost of fabricating fullerenes, it is not certain that this derivative can be synthesized on a large scale for commercial applications.

Proper names of oxidoreductases are formed as "donor:acceptor oxidoreductase"; however, other names are much more common. The common name is "donor dehydrogenase" when possible, such as glyceraldehyde-3-phosphate dehydrogenase for the second reaction above. Common names are also sometimes formed as "acceptor reductase", such as NAD+ reductase. "Donor oxidase" is a special case where O2 is the acceptor.

The materials are chosen to make the differences large enough that these local electric fields are strong, which splits excitons much more efficiently than single layer photovoltaic cells. The layer with higher electron affinity and ionization potential is the electron acceptor, and the other layer is the electron donor. This structure is also called a planar donor-acceptor heterojunction.

When bacteria grow in aerobic environments, the terminal electron acceptor (O2) is reduced to water by an enzyme called an oxidase. When bacteria grow in anaerobic environments, the terminal electron acceptor is reduced by an enzyme called a reductase. In mitochondria the terminal membrane complex (Complex IV) is cytochrome oxidase. Aerobic bacteria use a number of different terminal oxidases.

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor.

A.Jorgensen and C.J.Cleveland, National Council for Science and the environment, Washington DC using dissolved oxygen in the water as an electron acceptor.

MT-CO2 provides the substrate-binding site and contains the binuclear copper A center, probably the primary acceptor in cytochrome c oxidase.

Alpha-acceptor-substituted primary aliphatic amines R-CH2-NH2 (R = COOR, CN, CHO, COR) react with nitrous acid to generate the diazo compound.

The reagent is prepared from trimethylsilyl chloride and bromotrifluoromethane in the presence of a phosphorus(III) reagent that serves as a halogen acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with a copper protein as acceptor.

Several species of Pseudomonas, such as Pseudomonas aeruginosa are able to respire both aerobically and anaerobically, using nitrate as the terminal electron acceptor.

If the Acceptor accepted a proposal at some point in the past, it must include the previous proposal number, say m, and the corresponding accepted value, say w, in its response to the Proposer. :: Otherwise (that is, n is less than or equal to any previous proposal number received from any Proposer by the Acceptor) the Acceptor can ignore the received proposal. It does not have to answer in this case for Paxos to work. However, for the sake of optimization, sending a denial (Nack) response would tell the Proposer that it can stop its attempt to create consensus with proposal n.

Fig. 5: Sketch of a dispersed junction photovoltaic cell Bulk heterojunctions have an absorption layer consisting of a nanoscale blend of donor and acceptor materials. The domain sizes of this blend are on the order of nanometers, allowing for excitons with short lifetimes to reach an interface and dissociate due to the large donor-acceptor interfacial area. However, efficient bulk heterojunctions need to maintain large enough domain sizes to form a percolating network that allows the donor materials to reach the hole transporting electrode (Electrode 1 in Fig. 5) and the acceptor materials to reach the electron transporting electrode (Electrode 2).

In enzymology, a L-glutamate oxidase () is an enzyme that catalyzes the chemical reaction :L-glutamate + O2 \+ H2O \rightleftharpoons 2-oxoglutarate + NH3 \+ H2O2 The 3 substrates of this enzyme are L-glutamate, O2, and H2O, whereas its 3 products are 2-oxoglutarate, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-glutamate:oxygen oxidoreductase (deaminating). Other names in common use include glutamate (acceptor) dehydrogenase, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), and L-glutamic acid oxidase.

Most eukaryotic cells have mitochondria, which produce ATP from products of the citric acid cycle, fatty acid oxidation, and amino acid oxidation. At the inner mitochondrial membrane, electrons from NADH and FADH2 pass through the electron transport chain to oxygen, which is reduced to water. The electron transport chain comprises an enzymatic series of electron donors and acceptors. Each electron donor will pass electrons to a more electronegative acceptor, which in turn donates these electrons to another acceptor, a process that continues down the series until electrons are passed to oxygen, the most electronegative and terminal electron acceptor in the chain.

The reaction is also diastereoselective because the enamine addition occurs with a preference for trans addition without formation of the cis isomer. Scheme 2 regio- and diastereoselective Povarov reactionIn 2013, Doyle and coworkers reported a Povarov-type, formal [4+2]-cycloaddition reaction between donor- acceptor cyclopropenes and imines (Scheme 3). In the first step, a dirhodium catalyst effects diazo decomposition from silyl enol ether diazo compound to yield a donor/acceptor cyclopropene. The donor/acceptor cyclopropene is then reacted with an aryl imine under scandium(III) triflate catalyzed conditions to yield cyclopropane-fused tetrahydroquinolines in good yields and diastereoselectivities.

The colonies have a dirty yellow color that is best seen by smearing a colony on a piece of white paper. Requires either hydrogen or formate as an electron donor for growth. Grows under microaerophilic conditions (6% O2, 5% CO2, 15% H2, 74% N2) where O2 serves as the electron acceptor or anaerobic with fumarate as the terminal electron acceptor.

1-Hydroxycarotenoid 3,4-desaturase (, CrtD, hydroxyneurosporene desaturase, carotenoid 3,4-dehydrogenase, 1-hydroxy-carotenoid 3,4-dehydrogenase) is an enzyme with systematic name 1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction : 1-hydroxy-1,2-dihydrolycopene + acceptor \rightleftharpoons 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides acts primarily on acyclic carotenoids.

6-hydroxypseudooxynicotine dehydrogenase () is an enzyme with systematic name 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction: : 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O \rightleftharpoons 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor This enzyme contains a cytidylyl molybdenum cofactor.

It can also be used as a long-wavelength hetero-FRET (fluorescence resonant energy transfer) acceptor and probe for homo-FRET experiments. FRET is a type of fluorescence energy transfer where there is no intermediate photon and the energy is transferred from the donor to the acceptor. As well as be used to label bacteria to visualize them without antibiotic pressure.

HOMO to LUMO energy level. The electrons now in the LUMO energy level can travel to nearby acceptor molecules, which are more electronegative and thus lower in energy. The driving force for the electron transfer between donor and acceptor is the difference in LUMO energy levels. Polymer-fullerene bulk heterojunction solar cells are a type of solar cell researched in academic laboratories.

The different methods for treating VOF can be roughly divided into three categories, namely the donor-acceptor formulation, higher order differencing schemes and line techniques.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with an iron-sulfur protein as acceptor.

One such feature is the quantum Hall effect, seen at high magnetic fields. Acceptor dopants can also lead to a two- dimensional hole gas (2DHG).

The L2HGDH protein catalyzes the following reaction, and requires flavin adenine dinucleotide (FAD) as a co-factor: (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. L-2-hydroxyglutarate is produced by promiscuous action of malate dehydrogenase on 2-oxoglutarate; the L2HGDH protein is thus an example of a metabolite repair enzyme because it reconverts the useless damage product L-2-hydroxyglutarate back to 2-oxoglutarate.

Once all input has been received, if the current state is an accepting state, the input is accepted; otherwise it is rejected. As a rule, input is a sequence of symbols (characters); actions are not used. The start state can also be an accepting state, in which case the acceptor accepts the empty string. The example in figure 4 shows an acceptor that accepts the string "nice".

An abstract family of acceptors (AFA) is a grouping of generalized acceptors. Informally, an acceptor is a device with a finite state control, a finite number of input symbols, and an internal store with a read and write function. Each acceptor has a start state and a set of accepting states. The device reads a sequence of symbols, transitioning from state to state for each input symbol.

Delta8-fatty-acid desaturase (, Delta8-sphingolipid desaturase, EFD1, BoDES8, SLD, Delta8 fatty acid desaturase, Delta8-desaturase) is an enzyme with systematic name phytosphinganine,hydrogen donor:oxygen Delta8-oxidoreductase. This enzyme catalyses the following chemical reaction : phytosphinganine + reduced acceptor + O2 \rightleftharpoons Delta8-phytosphingenine + acceptor + 2 H2O This enzyme, which has been found mainly in plants, introduces a double bond at Delta8 of C18 and C20 fatty acids.

A good example is the bill acceptor. Initially, the bill acceptor was designed for vending machines as a means of selling candy to the public. It includes a device that recognizes that a US one dollar bank note has been inserted. The cleaning card was required to be the same shape as US currency in order to be accepted into the device to clean it.

Sulfur reduction uses sulfate as an electron acceptor for the assimilation of sulfur. Microbes that perform sulfate reduction typically use hydrogen, methane or organic matter as an electron donor. Anaerobic oxidation of methane (AOM) often use sulfate as electron acceptor. This method is favoured by organisms living in highly anoxic areas of the hydrothermal vent, thus are one of the predominate processes that occur within the sediments.

The reaction sequence in the related Hauser annulation is a Michael addition followed by a Dieckmann condensation and finally an elimination. The Dieckmann condensation is a similar ring closing intramolecular chemical reaction of diesters with base to give β-ketoesters. The Hauser donor is an aromatic sulfone or methylene sulfoxide with a carboxylic ester group in the ortho position. The Hauser acceptor is a Michael acceptor.

Separating and contacting (from a to b and from b to c) in atomic precision. Monolayer of a blue fluorescent dye (donor) on a glass slide partially covered by a monolayer of a red fluorescent dye (acceptor) fixed at a PVA-polymer layer. Energy transfer from donor to acceptor at contact.D. Möbius: "Manipulieren in molekularen Dimensionen" Chemie in unserer Zeit 9:173-182 (1975).

A hydrogen atom attached to a relatively electronegative atom is the hydrogen bond donor. C-H bonds only participate in hydrogen bonding when the carbon atom is bound to electronegative substituents, as is the case in chloroform, CHCl3. In a hydrogen bond, the electronegative atom not covalently attached to the hydrogen is named proton acceptor, whereas the one covalently bound to the hydrogen is named the proton donor. While this nomenclature is recommended by the IUPAC, it can be misleading, since in other donor-acceptor bonds, the donor/acceptor assignment is based on the source of the electron pair (such nomenclature is also used for hydrogen bonds by some authors).

Systematic names of transferases are constructed in the form of "donor:acceptor grouptransferase." For example, methylamine:L-glutamate N-methyltransferase would be the standard naming convention for the transferase methylamine-glutamate N-methyltransferase, where methylamine is the donor, L-glutamate is the acceptor, and methyltransferase is the EC category grouping. This same action by the transferase can be illustrated as follows: :methylamine + L-glutamate \rightleftharpoons NH3 \+ N-methyl-L-glutamate However, other accepted names are more frequently used for transferases, and are often formed as "acceptor grouptransferase" or "donor grouptransferase." For example, a DNA methyltransferase is a transferase that catalyzes the transfer of a methyl group to a DNA acceptor.

Fullerenes such as C60 and its derivatives are used as electron acceptor materials in bulk heterojunction photovoltaic cells. A cell with the blend of MEH-PPV and a methano- functionalized C60 derivative as the heterojunction, ITO and Ca as the electrodes showed a quantum efficiency of 29% and a power conversion efficiency of 2.9% under monochromatic illumination. Replacing MEH-PPV with P3HT produced a quantum yield of 45% under a 10 V reverse bias. Further advances in modifying the electron acceptor has resulted in a device with a power conversion efficiency of 10.61% with a blend of PC71BM as the electron acceptor and PTB7-Th as the electron donor.

In medicinal chemistry, parallel artificial membrane permeability assay (PAMPA) is a method which determines the permeability of substances from a donor compartment, through a lipid-infused artificial membrane into an acceptor compartment. A multi-well microtitre plate is used for the donor and a membrane/acceptor compartment is placed on top; the whole assembly is commonly referred to as a “sandwich”. At the beginning of the test, the drug is added to the donor compartment, and the acceptor compartment is drug-free. After an incubation period which may include stirring, the sandwich is separated and the amount of drug is measured in each compartment.

It is, however, important to keep the illumination the same for the with- and without-acceptor measurements, as photobleaching increases markedly with more intense incident light.

The state of the device can be determined by measuring the separation between donor and acceptor fluorophores using FRET. DNA walkers are another type of DNA machine.

In fact, the increase in gene transcription exhibits not only the increase in likelihood of it to be used as a donor but also as an acceptor.

Evolutionary conserved protein domain corresponding to oxidoreductase activity. NAD binding catalyzes redox reactions to alter the oxidation state of metal ions, using NADP+ as an electron acceptor.

In this acceptor, the only accepting state is state 7. A (possibly infinite) set of symbol sequences, called a formal language, is a regular language if there is some acceptor that accepts exactly that set. For example, the set of binary strings with an even number of zeroes is a regular language (cf. Fig. 5), while the set of all strings whose length is a prime number is not.

It was previously believed that methane and sulfate could not coexist due to the established hierarchy of metabolisms in sediments. In well-oxygenated sediments, oxygen is the main electron acceptor in aerobic respiration. Once all of the oxygen is consumed, organisms begin using substrates like nitrate, manganese oxides, and iron oxides as the electron acceptor in anaerobic respiration. However, these substrates tend to be low in concentrations throughout sediments.

Another challenge is high probability of exciton recombination in fullerenes-based electron acceptors. Contrary to the inorganic semiconductors, the excitons formed in organic materials possess a higher binding energy (0.3-1.0 eV). This issue is resolved at the acceptor donor interface by matching HOMO (donor) and LUMO (acceptor) energy gaps. Planar heterojunction (PHJ) is the commonly used OPV architecture in which donor and acceptors molecules are joined with one another.

Delta12-fatty-acid desaturase (, Delta12 fatty acid desaturase, Delta12(omega6)-desaturase, oleoyl-CoA Delta12 desaturase, Delta12 desaturase, Delta12-desaturase) is an enzyme with systematic name acyl-CoA,hydrogen donor:oxygen Delta12-oxidoreductase. This enzyme catalyses the following chemical reaction : acyl-CoA + reduced acceptor + O2 \rightleftharpoons Delta12-acyl-CoA + acceptor + 2 H2O In the yeast Lipomyces starkeyi and in the American cockroach, this microsomal enzyme converts oleoyl-CoA into linoleoyl- CoA.

Naqvi became a naturalized British citizen in 1974, but left Sheffield for the Physical Chemistry Laboratory, Swiss Federal Institute of Technology (ETH) in Zurich. In 1976, he reported the first example of a comparatively rare phenomenon: electronic energy transfer, mediated by electron exchange, from a triplet donor to a double acceptor; in his experiments, the donor was the benzophenone triplet and the acceptor was the benzophenone ketyl radical.

CuPc has often been investigated in the context of molecular electronics. It is potentially suited for organic solar cells because of its high chemical stability and uniform growth. CuPc usually plays the role of the electron donor in donor/acceptor based solar cells. One of the most common donor/acceptor architectures is CuPc/C60 (buckminsterfullerene) which rapidly became a model system for the study of small organic molecules.

This releases fructose and forms a sugar-enzyme intermediate when the glucose unit attaches to the nucleophile. The second displacement is transfer of a glucosyl moiety to an acceptor, such as a growing glucan chain. The debate in the past was over whether the glucosyl group attached to the non-reducing or reducing end of an incoming acceptor. Additional investigations pointed to a non-reducing mechanism with a single active site.

The compounds are employed for dehydrohalogenationMöller, Fr.; Oediger, H. "1,5-Diazabicyclo[5.4.0]undec-5-ene, a New Hydrogen Halide Acceptor" Angew. Chem. Int. Ed. Engl. , 1967, 5, 76.

In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase () is an enzyme that catalyzes the chemical reaction :(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor \rightleftharpoons (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor The 3 substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA, H2O, and acceptor, whereas its two products are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA, and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha- trihydroxy-5beta-cholestan-26-oyl-CoA:ac ceptor 24-oxidoreductase (24R-hydroxylating). Other names in common use include trihydroxycoprostanoyl- CoA oxidase, THC-CoA oxidase, THCA-CoA oxidase, 3alpha,7alpha,12alpha- trihydroxy-5beta-cholestanoyl-CoA oxidase, 3alpha,7alpha,12alpha- trihydroxy-5beta-cholestan-26-oate 24-hydroxylase.

The pharmacophore model for TRPV1 antagonists consists of three essential features: a hydrogen- bond acceptor, a hydrogen-bond donor, and a ring feature. In addition, the TRPV1 antagonists have been superimposed in such a way that they could fit in the volume of the TRPV1 pore. When the homology model is considered, appropriate interaction sites are found in the receptor pore. The hydrogen- bond acceptor on the ligand is proposed to interact with Tyr 667 (helix S6) on the receptor as a hydrogen-bond donor, and the hydrogen-bond donor on the ligand is proposed to interact with Tyr 667 on the opposite monomer of the tetramer on the receptor as a hydrogen-bond acceptor.

In enzymology, a NADH dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction :NADH + H+ \+ a quinone \rightleftharpoons NAD+ \+ a quinol The 3 substrates of this enzyme are NADH, H+, and a quinone (electron acceptor), whereas its two products are NAD+ and a quinol (reduced acceptor). This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase, NADH-quinone oxidoreductase, NADH ubiquinone oxidoreductase, DPNH-menadione reductase, D-diaphorase, and NADH2 dehydrogenase (quinone), and mitochondrial (mt) complex I. This enzyme participates in oxidative phosphorylation.

The Type II photosynthetic apparatus in non-oxygenic bacteria consists of light-harvesting protein- pigment complexes LH1 and LH2, which use carotenoid and bacteriochlorophyll as primary donors. LH1 acts as the energy collection hub, temporarily storing it before its transfer to the photosynthetic reaction centre (RC). Electrons are transferred from the primary donor via an intermediate acceptor (bacteriophaeophytin) to the primary acceptor (quinine Qa), and finally to the secondary acceptor (quinone Qb), resulting in the formation of ubiquinol QbH2. RC uses the excitation energy to shuffle electrons across the membrane, transferring them via ubiquinol to the cytochrome bc1 complex in order to establish a proton gradient across the membrane, which is used by ATP synthetase to form ATP.

Reduction of NAD+ to NADH. NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase. The chemical reaction these enzymes catalyze are generally represented with the follow equation; : NADH + H+ \+ acceptor NAD+ \+ reduced acceptor NADH dehydrogenase is a flavoprotein that contains iron-sulfur centers.

One can also do this by titrating protein with TNP- ATP in the presence and absence of varying concentrations of the ligand of interest. Using either experiment will allow the binding affinity of the ligand to protein to be measured. TNP-ATP is also valuable fluorescence acceptor. This is because, as with any good acceptor, TNP-ATP absorbs over a wide wavelength range that corresponds to the range of emission of common FRET donors.

Most organic bases are considered to be weak. Many factors can affect the strength of the compounds. One such factor is the inductive effect. A simple explanation of the term would state that electropositive atoms (such as carbon groups) attached in close proximity to the potential proton acceptor have an "electron-releasing" effect, such that the positive charge acquired by the proton acceptor is distributed over other adjacent atoms in the chain.

F. placidus was the first hyperthermophile discovered to grow anaerobically by oxidizing aromatic compounds such as benzoate coupled to the reduction of ferric iron (Fe3+) to ferrous iron (Fe2+). Hydrogen gas (H2) and sulfide (H2S) can also be used as energy sources. Due to its anaerobic lifestyle, nitrate (NO3−) is used as a terminal electron acceptor whereby it is converted to nitrite (NO2−). Thiosulfate (S2O32−) can also be used as a terminal electron acceptor.

With a variety of alkyl bromides oxidative addition can occur to yield the alkyltin tribromide e.g. :SnBr2 \+ RBr-> RSnBr3 Tin(II) bromide can act as a Lewis acid forming adducts with donor molecules e.g. trimethylamine where it forms NMe3·SnBr2 and 2NMe3·SnBr2 It can also act as both donor and acceptor in, for example, the complex F3B·SnBr2·NMe3 where it is a donor to boron trifluoride and an acceptor to trimethylamine.

In enzymology, an acyl-[acyl-carrier-protein] desaturase () is an enzyme that catalyzes the chemical reaction :stearoyl-[acyl-carrier-protein] + reduced acceptor + O2 \rightleftharpoons oleoyl-[acyl-carrier-protein] + acceptor + 2 H2O The systematic name of this enzyme class is acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase. Other names in common use include stearyl acyl carrier protein desaturase, and stearyl-ACP desaturase. This enzyme participates in polyunsaturated fatty acid biosynthesis. It employs one cofactor, ferredoxin.

APS and PAPS are intermediates in the reduction of sulfate to sulfite, an exothermic conversion that is carried out by sulfate-reducing bacteria. In these organisms, sulfate serves as an electron acceptor, akin to the use of O2 as an electron acceptor by aerobic organisms. Sulfate is not reduced directly but must be activated by the formation of APS or PAPS. These carriers of activated sulfate are produced by reaction with ATP.

Non-fullerene acceptors (NFAs) are types of acceptors used in organic solar cells (OSCs). The name Fullerene comes from another type of acceptor-molecule which was used as the main acceptor material for bulk heterojunction Organic solar cells. Non-fullerene acceptors are thus defined as not being a part of this sort of acceptors. Research in non-fullerene acceptors did not show promising results starting up when being compared to fullerene based organic solar cells.

In biological systems, FAD acts as an acceptor of H+ and e− in its fully oxidized form, an acceptor or donor in the FADH form, and a donor in the reduced FADH2 form. The diagram below summarizes the potential changes that it can undergo. :422px Along with what is seen above, other reactive forms of FAD can be formed and consumed. These reactions involve the transfer of electrons and the making/breaking of chemical bonds.

The antibody, originally called G5/44, was created by grafting the complementarity-determining regions and some framework residues from the murine anti-CD22 mAb m5/44, onto human acceptor frameworks.

While the oxygen slowly dissociates, it is theorized that it may then act to displace the sulfate that normally acts as the terminal electron acceptor in their electron transport chain.

Then FADH2 is oxidized by the final electron acceptor, molecular oxygen (O2), which can do so because it has a higher reduction potential. O2 is then reduced to hydrogen peroxide (H2O2).

Sulfotransferases (SULTs) are transferase enzymes that catalyze the transfer of a sulfo group from a donor molecule to an acceptor alcohol or amine. The most common sulfo group donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In the case of alcohol as acceptor, the product is a sulfate (R-OSO3−), whereas an amine leads to a sulfamate (R-NH-SO3−). Both reactive groups for a sulfonation via sulfotransferases may be part of a protein, lipid, carbohydrate or steroid.

Another way to design an orthogonal protein is to switch the position of the hydrogen bond acceptors and donors. For example, if the ligand is a hydrogen bond donor and the protein a hydrogen bond acceptor, switch the ligand to the hydrogen bond acceptor and the protein to the donor. The reversal of charged interactions is similar, but it involves switching the position of the positive charge and the negative charge on the protein and ligand.

The donor- acceptor scheme is based on two fundamental criteria, namely the boundedness criterion and the availability criterion. The first one states that the value of C has to be bounded between zero and one. The latter criterion ensures that the amount of fluid convected over a face during a time step is less than or equal to the amount available in the donor cell, i.e., the cell from which the fluid is flowing to the acceptor cell.

In semiconductor physics, an acceptor is a dopant atom that when added to a semiconductor can form a p-type region. Boron atom acting as an acceptor in the simplified 2D silicon lattice. For example, when silicon (Si), having four valence electrons, needs to be doped as a p-type semiconductor, elements from group III like boron (B) or aluminium (Al), having three valence electrons, can be used. The latter elements are also called trivalent impurities.

For example, an enzyme that catalyzed this reaction would be an oxidoreductase: :A- \+ B -> A + B- In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis: :Pi \+ glyceraldehyde-3-phosphate + NAD+ -> NADH + H+ \+ 1,3-bisphosphoglycerate In this reaction, NAD+ is the oxidant (electron acceptor), and glyceraldehyde-3-phosphate is the reductant (electron donor).

Organic conductors consist of donor and acceptor molecules building separated planar sheets or columns. The energy difference in the ionization energy acceptor and the electron affinity of the donor leads to a charge transfer and consequently to free carriers whose number is normally fixed. The carriers are delocalized throughout the crystal due to the overlap of the molecular orbitals being also reasonable for the high anisotropic conductivity. That is why it will be distinct between different dimensional organic conductors.

A chemical glycosylation reaction involves the coupling of a glycosyl donor, to a glycosyl acceptor forming a glycoside.Crich, D.; Lim, L. Org. React. 2004, 64, 115. Bufali, S.; Seeberger, P. Org. React.

It has a XLogP3 value of 3.4. Its hydrogen bond donor count is 2 and its hydrogen bond acceptor is 3. Its surface area is 41.5 Å² and has 18 heavy atoms.

So lysidine allows better translation fidelity. :Lysidine base pairs with Adenosine in context of a Cytidine to Guanosine base pair. R = ribose. Arrows indicate hydrogen bonds going from hydrogens to bond acceptor.

Under aerobic conditions, the microorganisms will use oxygen as an electron acceptor. The resulting products are carbon dioxide (CO2) and water (H2O). Examples of aerobic conditions for microbial biodegradation include landfills and sediments.

This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. This enzyme participates in ascorbate metabolism. It employs one cofactor, copper.

The second tRNA binding sequence, the T box sequence, is complementary to the nucleotide preceding the acceptor end of the tRNA. The T box is found in the side bulge of the antiterminator.

Takeshi Todo, a former brainwashed servant of Khan, reflects on the past incidents as monster attacks took place in real life. Using the Acceptor, he transforms into Gridman Sigma before facing the monster.

When outrons are processed, the SL exon is trans-spliced to distinct, unpaired, downstream acceptor sites adjacent to each open reading frame of the polycistronic pre-mRNA, leading to distinct mature capped transcripts.

Under low microbial population densities, usage of electron shuttles and chelators synthesized by the exoelectrogen may be energetically costly due to insufficient concentrations of such molecules required for recovery and reuse. Under these circumstances, direct transfer would be favored; however, energy benefits would outweigh energy demands when the microbial community is of sufficient size. Direct reduction of an exogenous acceptor is achieved through contact between the cell’s oxidoreductases and the terminal electron acceptor (i.e. an electrode or external metal compound).

The two components will self-assemble into an interpenetrating network connecting the two electrodes. They are normally composed of a conjugated molecule based donor and fullerene based acceptor. The nanostructural morphology of bulk heterojunctions tends to be difficult to control, but is critical to photovoltaic performance. After the capture of a photon, electrons move to the acceptor domains, then are carried through the device and collected by one electrode, and holes move in the opposite direction and collected at the other side.

Vending machines began accepting higher denominations as well as having the ability to make change. Specialized sensors were introduced into the bill acceptors to recognize multiple denominations and to only accept media that contained bank note characteristics. The bill acceptor cleaning card was redeveloped to contain magnetic ink and bank note characteristics so as to be accepted by the equipment. The development of bill acceptors for slot machines in the gaming and casino industry required the bill acceptor to be more sophisticated.

In enzymology, a chlorate reductase () is an enzyme that catalyzes the chemical reaction :AH2 \+ chlorate \rightleftharpoons A + H2O + chlorite Thus, the two substrates of this enzyme are a reduced electron acceptor (denoted AH2) and chlorate, whereas its 3 products are an oxidized electron acceptor (denoted A), water, and chlorite. It is closely related to the enzyme perchlorate reductase which reduces both chlorate and perchlorate. This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is chlorite:acceptor oxidoreductase.

In enzymology, a hydrogenase (acceptor) () is an enzyme that catalyzes the chemical reaction :H2 \+ A \rightleftharpoons AH2 Thus, the two substrates of this enzyme are H2 and A, whereas its product is AH2. This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with other acceptors. The systematic name of this enzyme class is hydrogen:acceptor oxidoreductase. Other names in common use include H2 producing hydrogenase[ambiguous], hydrogen-lyase[ambiguous], hydrogenlyase[ambiguous], uptake hydrogenase[ambiguous], and hydrogen:(acceptor) oxidoreductase.

Rylene diimides are, as said, one of the two main subclasses which are a basis for acceptor-molecules in modern NFA-OSCs. Rylene diimides are industrial dyes and can be divided into, once again, two subclasses: Perylene Diimides (PDIs) and Naphthalene Diimides (NDIs). Rylene diimides consist of a planar rylene framework and numerous constructions can be made by attaching certain subgroups and by using more PDI molecules in one acceptor. The mono- PDI molecule is shown in the figure on the right.

Based on the split gene theory, Senapathy developed computational algorithms to detect the donor and acceptor splice sites, exons and a complete split gene in a genomic sequence. He developed the position weight matrix (PWM) method based on the frequency of the four bases at the consensus sequences of the donor and acceptor in different organisms to identify the splice sites in a given sequence. Furthermore, he formulated the first algorithm to find the exons based on the requirement of exons to contain a donor sequence (at the 5’ end) and an acceptor sequence (at the 3’ end), and an ORF in which the exon should occur, and another algorithm to find a complete split gene. These algorithms are collectively known as the Shapiro- Senapathy algorithm (S&S;).

In standard cis-splicing, the donor splice site in upstream position is required together with an acceptor site located on downstream position on the same pre-RNA molecule. By contrast, the SL trans- splicing relies on a 3' acceptor splice site on the outron, and a 5' donor splice site (GU dinucleotide) located on a separate RNA molecule, the SL RNA. Moreover, the outron of the premature mRNA contains a branchpoint adenosine — followed by a downstream polypyrimidine tract — which interacts with the intron-like portion of the SL RNA to form a 'Y' branched byproduct, reminiscent of the lasso structure formed during intron splicing. Nuclear machinery then resolves this 'Y' branching structure by trans-splicing the SL RNA sequence to the 3′ trans-splice acceptor site (AG dinucleotide) of the pre-mRNA.

Acceptor-type hydrogen bonds (terminating on an oxygen's lone pairs) are more likely to form bifurcation (it is called overcoordinated oxygen, OCO) than are donor-type hydrogen bonds, beginning on the same oxygen's hydrogens.

The first stable subvalent Be complex ever observed contains a three-center two-electron π-bond that consists of donor-acceptor interactions over the C-Be-C core of a Be(0)-carbene adduct.

Belongs to the oxidoreductase family, oxidizing metal ions with NADP+ acting as an electron acceptor. Uses FAD as a cofactor when catalyzing the following reaction: 2cob(II)alamin + NADP+ 2aquacob(III)alamin + NADPH + H+.

This makes them less compatible for bulk heterojunction blends than FAs. Another downside to research on SMA usage is the profound scala of possibilities of donor-acceptor pairs that scientists are challenged to induce.

In its most common setting, the HAMP domain transmits conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains and thus regulates the phosphorylation or methylation activity of homodimeric receptors.

Brock Biology of Microorganisms (13 ed.). San Francisco: Pearson Education Inc. However D. lykanthroporepellens uses polychlorinated aliphatic alkanes as the electron acceptor. Chloroflexi are the deepest branching (oldest) anoxygenic phototrophs on the tree of life.

The second donor acts solely to absorb light, transferring extra energy to the first donor material. In parallel linkage, both donors produce excitons independently, which then migrate to their respective donor/acceptor interfaces and dissociate.

When no Salmonella is present, the Ab-QDs function as the donor, with graphene being the acceptor, and the fluorescence of the test line is quenched by this energy transfer. The presence of Salmonella, on the other hand, allows for fluorescence because of the manner in which the bacterial cells bind to the Ab-QDs: the distance between the donor and acceptor is too large to allow for the energy transfer, and thus fluorescence is not quenched. The strips have a detection limit of 100 CFU/mL.

Delta11-fatty-acid desaturase (, Delta11 desaturase, fatty acid Delta11-desaturase, TpDESN, Cro-PG, Delta11 fatty acid desaturase, Z/E11-desaturase, Delta11-palmitoyl-CoA desaturase) is an enzyme with systematic name acyl-CoA,hydrogen donor:oxygen Delta11-oxidoreductase. This enzyme catalyses the following chemical reaction : acyl-CoA + reduced acceptor + O2 \rightleftharpoons Delta11-acyl-CoA + acceptor + 2 H2O The enzyme from the marine microalga Thalassiosira pseudonana desaturates palmitic acid 16:0 to 16:1Delta11, whereas that from the leafroller moth Choristoneura rosaceana desaturates myristic acid 14:0 to 14:1Delta11.

CPPs are unique in that their donor–acceptor properties can be adjusted with the addition or removal of each phenyl ring. In the all-carbon nano-hoop systems a reduction in width corresponds to a higher HOMO and a lower LUMO. Additional donor–acceptor selectivity was observed by the addition of an aromatic heterocycles into the larger ring. N-methylaza[n]CPP showed that a lowering of the LUMO could be enhanced by decreasing the ring size, while the HOMO energy level remained the same.

In enzymology, a malate dehydrogenase (quinone) (), formerly malate dehydrogenase (acceptor) (EC 1.1.99.16), is an enzyme that catalyzes the chemical reaction :(S)-malate + a quinone \rightleftharpoons oxaloacetate + reduced quinone Thus, the two substrates of this enzyme are (S)-malate and a quinone, whereas its two products are oxaloacetate and reduced quinone. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone as acceptor. The systematic name of this enzyme class is (S)-malate:quinone oxidoreductase.

Phosphoribulokinase (PRK) () is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle. Its main function is to regenerate RuBP, which is the initial substrate and CO2-acceptor molecule of the Calvin Cycle. PRK belongs to the family of transferase enzymes, specifically those transferring phosphorus-containing groups (phosphotransferases) to an alcohol group acceptor. Along with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCo), phosphoribulokinase is unique to the Calvin Cycle.

The catalysis of this mechanism is initiated by the deprotonation of TPP at the thiazolium ring. This carbanion then binds to the carbonyl of the donor substrate thus cleaving the bond between C-2 and C-3. This keto fragment remains covalently bound to the C-2 carbon of TPP. The donor substrate is then released, and the acceptor substrate enters the active site where the fragment, which is bound to the intermediate α-β-dihydroxyethyl thiamin diphosphate, is then transferred to the acceptor.

Sequencers (also called generators) are a subclass of acceptors and transducers that have a single-letter input alphabet. They produce only one sequence which can be seen as an output sequence of acceptor or transducer outputs.

Sulfur reduction occurs in plants, fungi, and many bacteria."Pathway: sulfate reduction I (assimilatory)." MetaCyc. Sulfate can serve as an electron acceptor in anaerobic respiration and can also be reduced for the formation of organic compounds.

For device applications, the aspirational oxidant is a photovoltaic material. For screening WOCs, ceric ammonium nitrate is a typical electron acceptor. Solar panels are the aspirational power sources for driving water splitting, including water oxidation catalysis.

Intramolecular hydrogen bonding of an ortho OH donor to the carbonyl oxygen of the carboxyl group, acting as an acceptor, increases the positive charge on the carbonyl carbon and consequently the acidity of the carboxyl OH.

In the semiconductor at the smaller voltage shown in the top panel, the positive charge placed on the left face of the insulator lowers the energy of the valence band edge. Consequently, these states are fully occupied out to a so-called depletion depth where the bulk occupancy reestablishes itself because the field cannot penetrate further. Because the valence band levels near the surface are fully occupied due to the lowering of these levels, only the immobile negative acceptor-ion charges are present near the surface, which becomes an electrically insulating region without holes (the depletion layer). Thus, field penetration is arrested when the exposed negative acceptor ion charge balances the positive charge placed on the insulator surface: the depletion layer adjusts its depth enough to make the net negative acceptor ion charge balance the positive charge on the gate.

This family includes glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) (CAZY GH_70) which catalyse the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules. Some members of this family contain a cell wall-binding repeat.

The term, according to some, is derived from the theme of the word "acceptor", which in Latin is Accipiter. For others, it stems from the symbol of the country, to accept a small plot of land, etc.

The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Nelson, J. (1970) Hydrogen-bonded complexes of isocyanic acid: Infrared spectra and thermodynamic measurements. Spectrochimica Acta Part A: Molecular Spectroscopy 26,109-120. The acceptor properties of HNCO are compared with other Lewis acid in the ECW model.

Another example, a molecule or atom that has a more positive value of electron affinity than another is often called an electron acceptor and the less positive an electron donor. Together they may undergo charge-transfer reactions.

Ammonia incorporation in animals and microbes occurs through the actions of glutamate dehydrogenase and glutamine synthetase. Glutamate plays the central role in mammalian and microbe nitrogen flow, serving as both a nitrogen donor and a nitrogen acceptor.

Pseudomonas and Halomonas are examples of the many thiobacteria that utilize thiosulfate dehydrogenase to derive energy from thiosulfate as a supplemental energy source. Tetrathionate can serve as a respiratory electron acceptor during anaerobic respiration by tetrathionate reduction.

The Sxl protein is a splicing repressor that binds to an ISS in the RNA of the Tra transcript near the upstream acceptor site, preventing U2AF protein from binding to the polypyrimidine tract. This prevents the use of this junction, shifting the spliceosome binding to the downstream acceptor site. Splicing at this point bypasses the stop codon, which is excised as part of the intron. The resulting mRNA encodes an active Tra protein, which itself is a regulator of alternative splicing of other sex-related genes (see dsx above).

Molecular rectifiers are mimics of their bulk counterparts and have an asymmetric construction so that the molecule can accept electrons in one end but not the other. The molecules have an electron donor (D) in one end and an electron acceptor (A) in the other. This way, the unstable state D+ – A− will be more readily made than D− – A+. The result is that an electric current can be drawn through the molecule if the electrons are added through the acceptor end, but less easily if the reverse is attempted.

A host–guest complex, also known as a donor–acceptor complex, may be formed from a Lewis base, B, and a Lewis acid, A. The host may be either a donor or an acceptor. In biochemistry host–guest complexes are known as receptor-ligand complexes; they are formed primarily by non-covalent bonding. Many host–guest complexes has 1:1 stoichiometry, but many others have more complex structures. The general equilibrium can be written as :p A + q B ApBq The study of these complexes is important for supramolecular chemistry and molecular recognition.

This means that the solvent arrangement with half of the electron on both donor and acceptor would be the correct environment for jumping. Also, in this state the energy of precursor and successor in their solvent environment would be the same. However, the electron as an elementary particle cannot be divided, it resides either on the donor or the acceptor and arranges the solvent molecules accordingly in an equilibrium. The "transition state", on the other hand, requires a solvent configuration which would result from the transfer of half an electron, which is impossible.

The ability of Lewis acids to coordinate to transition metals as σ-acceptor ligands was recognized as early as in the 1970s, but the so-called Z-type ligands remained curiosities until the early 2000s. Over the last decade, significant progress has been made in this area, especially via the incorporation of Lewis acid moieties into multidentate, ambiphilic ligands. The understanding of the nature and influence of metal→Z-ligand interactions has considerably improved and the scope of Lewis acids susceptible to behave as σ-acceptor ligands has been significantly extended.

The active region of an organic device consists of two materials, one electron donor and one electron acceptor. When a photon is converted into an electron hole pair, typically in the donor material, the charges tend to remain bound in the form of an exciton, separating when the exciton diffuses to the donor-acceptor interface, unlike most other solar cell types. The short exciton diffusion lengths of most polymer systems tend to limit the efficiency of such devices. Nanostructured interfaces, sometimes in the form of bulk heterojunctions, can improve performance.

Charge separation occurs at the donor-acceptor interface. Whilst traveling to the electrode, a charge can become trapped and/or recombine in a disordered interpenetrating organic material, resulting in decreased device efficiency. Controlled growth of the heterojunction provides better control over positions of the donor-acceptor materials, resulting in much greater power efficiency (ratio of output power to input power) than that of planar and highly disoriented hetero-junctions (as shown in Fig 5). Thus, the choice of suitable processing parameters in order to better control the structure and film morphology is highly desirable.

DHODH can vary in cofactor content, oligomeric state, subcellular localization, and membrane association. An overall sequence alignment of these DHODH variants presents two classes of DHODHs: the cytosolic Class 1 and the membrane-bound Class 2. In Class 1 DHODH, a basic cysteine residue catalyzes the oxidation reaction, whereas in Class 2, the serine serves this catalytic function. Structurally, Class 1 DHODHs can also be divided into two subclasses, one of which forms homodimers and uses fumarate as its electron acceptor, and the other which forms heterotetramers and uses NAD+ as its electron acceptor.

In many chemical circumstances, however, the transfer of electronic charge to an electron acceptor may be only fractional, meaning an electron is not completely transferred, but results in an electron resonance between the donor and acceptor. This leads to the formation of charge transfer complexes in which the components largely retain their chemical identities. The electron donating power of a donor molecule is measured by its ionization potential which is the energy required to remove an electron from the highest occupied molecular orbital. The overall energy balance (ΔE), i.e.

For Fermi levels below a sertain value EFre (for CGS this is the valence band maximum energy plus 0.2 eV) the defect acts as a shallow donor and causes a defect level at the conduction band. When the Fermi levels rise above EFre, the configuration of the defect changes into two states: a shallow acceptor and a deep acceptor. As a consequence of these defect levels, a nonuniform charge en and defect distribution is created which are affected by light and hence change various electrical characteristics of the module.

Tertiary alcohols form the products 6 and 7 via a SN1 mechanism. The driving force behind this and similar reactions is the formation of the strong PO double bond. The reaction is somewhat similar to the Mitsunobu Reaction, where the combination of an organophosphine as an oxide acceptor, an azo compound as a hydrogen acceptor reagent, and a nucleophile are used to convert alcohols to esters and other applications like this. The mechanism of the Appel reaction Illustrative use of the Appel reaction is the chlorination of geraniol to geranyl chloride.

The original procedure of the Robinson annulation begins with the nucleophilic attack of a ketone in a Michael reaction on a vinyl ketone to produce the intermediate Michael adduct. Subsequent aldol type ring closure leads to the keto alcohol, which is then followed by dehydration to produce the annulation product. In the Michael reaction, the ketone is deprotonated by a base to form an enolate nucleophile which attacks the electron acceptor (in red). This acceptor is generally an α,β-unsaturated ketone, although aldehydes, acid derivatives and similar compounds can work as well (see scope).

This finding provides more support for the dependence of halogen bonding on atomic polarizability. Utilizing similar donor-acceptor frameworks, the authors demonstrated that halogen bonding strength in the liquid crystalline state is comparable to the hydrogen-bonded mesogens.

H-bonds can also be measured by IR vibrational mode shifts of the acceptor. The amide I mode of backbone carbonyls in α-helices shifts to lower frequencies when they form H-bonds with side-chain hydroxyl groups.

EDMR has been demonstrated on a single electron from a quantum dot. Measurements of less than 100 donors and theoretical analyses of such a measurement have been published, relying on the Pb interface defect to act as the acceptor.

Bacteriovorax and Bdellovibrio are approximately 0.2-0.4 x 0.5-1.4 μm, are aerobic, with oxygen as a terminal electron acceptor, and are mesophilic. They display a typical Gram-negative morphology and are motile by a single, polar, sheathed flagellum.

Due to the sensitive location of splice sites, mutations in the acceptor or donor areas of splice sites can become detrimental to a human individual. In fact, many different types of diseases stem from anomalies within the splice sites.

Many applications and instruments were developed specifically for Allophycocyanin. It is commonly used in immunoassays such as FACS, flow cytometry, and High Throughput Screening as an acceptor for Europium via Time Resolved-Fluorescence Resonance Energy Transfer (TR-FRET) assays.

Bioremediation requires careful evaluation and design in accordance with existing conditions. Some sites may require the addition of an electron acceptor while others require microbe supplementation (bioaugmentation). Regardless of the method used, only constant monitoring can prevent future contamination.

Chrysiogenes arsenatis is a species of bacterium in the family Chrysiogenaceae. It has a unique biochemistry. Instead of respiring with oxygen, it respires using the most oxidized form of arsenic, arsenate. It uses arsenate as its terminal electron acceptor.

Therefore, in light, the electron acceptor is reduced and oxygen is evolved. Samuel Ruben and Martin Kamen used radioactive isotopes to determine that the oxygen liberated in photosynthesis came from the water. Melvin Calvin works in his photosynthesis laboratory.

The electron donor and acceptor are mixed in such a way that the gradient is gradual. This architecture combines the short electron travel distance in the dispersed heterojunction with the advantage of the charge gradient of the bilayer technology.

Tetracyanoquinodimethane (TCNQ) is the organic compound with the formula (NC)2CC6H4C(CN)2. This cyanocarbon, a relative of para-quinone, is an electron acceptor that is used to prepare charge transfer salts, which are of interest in molecular electronics.

It is possible for catalysis to occur with only one of the two substrates. If either acetyl-CoA or acetylcarnitine binds to CRAT, a water molecule may fill the other binding site and act as an acetyl group acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway.

This organism uses oxygen its preferred terminal electron acceptor and uses organic compounds for its carbon and energy source. No motility was observed. H. turkmenica tested positive for both oxidase and catalase activity. Also according to Selim et al.

The attractive nature of halogen bonds result in the distance between the donor and acceptor to be shorter than the sum of van der Waals radii. The XB interaction becomes stronger as the distance decreases between the halogen and Lewis base.

In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase. Dietary L-aspartic acid has been shown to act as an inhibitor of Beta-glucuronidase, which serves to regulate enterohepatic circulation of bilirubin and bile acids.

Under such conditions, Loxodes is able to use nitrate instead of oxygen as an electron acceptor for respiration. Nitrate respiration is rare among eukaryotes, and Loxodes was the first eukaryote known to have this capability. Loxodes is also sensitive to light.

F. acidophilum obtains energy by oxidation of the ferrous iron in pyrite using oxygen as a terminal electron acceptor. This process produces sulfuric acid as a by-product, leading to further acidification of its environment. Its type strain is YT.

The highest demonstrated efficiency is 3.2%, based upon a PCPDTBT polymer donor and CdSe nanoparticle acceptor. The device exhibited a short circuit current of 10.1 mA·cm−2, an open circuit voltage of .68 V, and a fill factor of .51.

Cycle for methanogenesis, showing intermediates. Methanogenesis in microbes is a form of anaerobic respiration. Methanogens do not use oxygen to respire; in fact, oxygen inhibits the growth of methanogens. The terminal electron acceptor in methanogenesis is not oxygen, but carbon.

532=2A>T and occurs in intron 7. This also destroys the splice donor and acceptor sites due to the inclusion of 83 extra nucleotides before exon 8 in the mRNA. This mutation causes non-sense mediated decay of the mRNA.

The domain is associated with the oxidoreductase family and acts on NADH or NADPH, using a heme protein as an electron acceptor. Requires FAD and FMN as cofactors to catalyse the reaction: NADPH + H+ + n oxidised hemoprotein = NADP+ + n reduced hemoprotein.

When exposed to microaerophilic conditions as found near deep sea hydrothermal vents, P. marina was able to perform aerobic respiration. Oxygen is not the primary electron acceptor and can only be utilized when exposed to oxygen in this microaerophilic environment.

Treatment of these compounds with TBAF invokes a ring- expansion that provides the corresponding benzazepines. Donor-acceptor cyclopropene formation and subsequent [4+2] cycloaddition to yield cyclopropane-fused tetrahydroquinolines. Subsequent treatment with TBAF opens the cyclopropane ring to give benzazepines.

In all cases the energy liberated is transferred to the electron transport chain for ATP and NADH production. In addition to aerobic sulfur oxidation, some organisms (e.g. Thiobacillus denitrificans) use nitrate () as a terminal electron acceptor and therefore grow anaerobically.

377Khanna, Pragya (2008). Cell and Molecular Biology, p. 151 Expressed as: :2 H2A + CO2 → 2A + CH2O + H2O where A is the electron acceptor. His discovery predicted that H2O is the hydrogen donor in green plant photosynthesis and is oxidized to O2.

Comparison between hydrogen and halogen bonding: ;Hydrogen bonding: A \cdots H-D ;Halogen bonding: A \cdots X-D In both cases, A (the hydrogen/halogen bond acceptor) is the atom, group, or molecule that donates electrons to the electron poor species H-D or X-D (the hydrogen or halogen bond donors respectively). H is the hydrogen atom involved in hydrogen bonding, and X is the halogen atom involved in halogen bonding. Note the halogen bond donor accepts electrons while the halogen bond acceptor donates electrons. A parallel relationship can easily be drawn between halogen bonding and hydrogen bonding (HB).

A fucosyltransferase is an enzyme that transfers an L-fucose sugar from a GDP- fucose (guanosine diphosphate-fucose) donor substrate to an acceptor substrate. The acceptor substrate can be another sugar such as the transfer of a fucose to a core GlcNAc (N-acetylglucosamine) sugar as in the case of N-linked glycosylation, or to a protein, as in the case of O-linked glycosylation produced by O-fucosyltransferase. There are various fucosyltransferases in mammals, the vast majority of which, are located in the Golgi apparatus. The O-fucosyltransferases have recently been shown to localize to the endoplasmic reticulum (ER).

It lowers the plateau of the action potential, decreasing the duration and the concentration parameters in the heart muscle cells. It has been seen that the 16-kDa subunit exhibits phospholipase activity, inducing a release of acyl CoA and acyl carnitine, fact which has a negative effect on cell’s integrity and function. TCX is involved in the outer hair cell motility too, by blocking the calcium traffic and preventing the cell shortening and elongation. Taicatoxin has an inhibitory effect by reducing the affinity of 125I-apamin for its acceptor and not by alteration of the acceptor binding site density.

G. ahangari is an anaerobe, using poorly soluble ferric iron (Fe3+) as a terminal electron acceptor. It can grow either autotrophically using hydrogen gas (H2) or heterotrophically using a large number of organic compounds, including several types of fatty acids, as energy sources. G. ahangari was the first archaeon isolated capable of using hydrogen gas coupled to iron reduction as an energy source and the first anaerobe isolated capable of using long-chain fatty acids as an energy source. A second species was described as G. acetivorans, which also uses iron as its terminal electron acceptor.

Certain antibiotics, such as tetracyclines, prevent the aminoacyl-tRNA from binding to the ribosomal subunit in prokaryotes. It is understood that tetracyclines inhibit the attachment of aa-tRNA within the acceptor (A) site of prokaryotic ribosomes during translation. Tetracyclines are considered broad-spectrum antibiotic agents; these drugs exhibit capabilities of inhibiting the growth of both gram-positive and gram-negative bacteria, as well as other atypical microorganisms. Furthermore, the TetM protein () is found to allow aminoacyl- tRNA molecules to bind to the ribosomal acceptor site, despite being concentrated with tetracyclines that would typically inhibit such actions.

In practice, FRET systems are characterized by the Förster's radius (R0): the distance between the fluorophores at which FRET efficiency is 50%. For many FRET parings, R0 lies between 20 and 90 Å, depending on the acceptor used and the spatial arrangements of the fluorophores within the assay. Through measurement of this energy transfer, interactions between biomolecules can be assessed by coupling each partner with a fluorescent label and detecting the level of energy transfer. Acceptor emission as a measure of energy transfer can be detected without needing to separate bound from unbound assay components (e.g.

Perchlorate reducatase is an enzyme that catalyzes the chemical reactions: :ClO4− \+ 2 AH2 \rightleftharpoons ClO2− \+ 2 A + 2 H2O and :ClO3− \+ AH2 \rightleftharpoons ClO2− \+ A + H2O Thus, the substrates of this enzyme are a reduced electron acceptor (denoted AH2) and either chlorate or perchlorate, sometimes collectively denoted as (per)chlorate. The products are chlorite, an oxidized electron acceptor (denoted A), and water. It is closely related to the enzyme chlorate reductase, but is distinguished by its ability to reduce both perchlorate and chlorate, whereas chlorate reductase only acts on chlorate. Perchlorate reductase and chlorate reductase are closely related but form genetically distinct clades.

In many chemical circumstances, however, the transfer of electronic charge from an electron donor may be only fractional, meaning an electron is not completely transferred, but results in an electron resonance between the donor and acceptor. This leads to the formation of charge transfer complexes in which the components largely retain their chemical identities. The electron accepting power of an acceptor molecule is measured by its electron affinity which is the energy released when filling the lowest unoccupied molecular orbital (LUMO). The energy required to remove one electron from the electron donor is its ionization energy (I).

In fluorescence microscopy, fluorescence confocal laser scanning microscopy, as well as in molecular biology, FRET is a useful tool to quantify molecular dynamics in biophysics and biochemistry, such as protein-protein interactions, protein–DNA interactions, and protein conformational changes. For monitoring the complex formation between two molecules, one of them is labeled with a donor and the other with an acceptor. The FRET efficiency is measured and used to identify interactions between the labeled complexes. There are several ways of measuring the FRET efficiency by monitoring changes in the fluorescence emitted by the donor or the acceptor.

The menaquinone, with the help of another enzyme, then transfers these two electrons to a suitable oxidant, such as fumarate or nitrate (also called an electron acceptor). Adding two electrons to fumarate or nitrate converts the molecule to succinate or nitrite plus water, respectively. Some of these reactions generate a cellular energy source, ATP, in a manner similar to eukaryotic cell aerobic respiration, except the final electron acceptor is not molecular oxygen, but fumarate or nitrate. In aerobic respiration, the final oxidant is molecular oxygen, which accepts four electrons from an electron donor such as NADH to be converted to water.

Class II oxidases are Quinol oxidases and can use a variety of terminal electron acceptors. Both of these classes can be subdivided into categories based on what redox active components they contain. E.g. Heme aa3 Class 1 terminal oxidases are much more efficient than Class 2 terminal oxidases Anaerobic bacteria, which do not use oxygen as a terminal electron acceptor, have terminal reductases individualized to their terminal acceptor. For example, E. coli can use fumarate reductase, nitrate reductase, nitrite reductase, DMSO reductase, or trimethylamine-N-oxide reductase, depending on the availability of these acceptors in the environment.

The entrance to the active site for this enzyme is made up mainly of several arginine, histidine, serine, and aspartate side-chains, with a glutamate side-chain playing a secondary role. These side-chains, to be specific Arg359, Arg528, His469, and Ser386, are conserved within each transketolase enzyme and interact with the phosphate group of the donor and acceptor substrates. Because the substrate channel is so narrow, the donor and acceptor substrates cannot be bound simultaneously. Also, the substrates conform into a slightly extended form upon binding in the active site to accommodate this narrow channel.

The research field of organic solar cells (OSC) is divided in two parts. Most scientists use wet chemical methods applying polymer materials as one of the two components to form the absorber layer of the devices, whereas the use of small absorber molecules deposited by vacuum thermal evaporation techniques is rather a niche of the field. However, in both concepts C60 is the other important component of the absorber because of its extraordinary electron acceptor properties. In 2002 Fostiropoulos presented a bi-layer heterojunction absorber concept with Zn-phthalocyanine and C60 molecules as donor and acceptor materials, respectively.

The outron is an intron-like sequence possessing similar characteristics such as the G+C content and a splice acceptor site that is the signal for trans-splicing. Such a trans-splice site is essentially defined as an acceptor (3') splice site without an upstream donor (5') splice site. In eukaryotes such as euglenozoans, dinoflagellates, sponges, nematodes, cnidarians, ctenophores, flatworms, crustaceans, chaetognaths, rotifers, and tunicates, the length of spliced leader (SL) outrons range from 30 to 102 nucleotides (nt), with the SL exon length ranging from 16 to 51 nt, and the full SL RNA length ranging from 46 to 141 nt.

Other names for glycerol-3-phosphate dehydrogenase include alpha-glycerophosphate dehydrogenase, alpha-glycerophosphate dehydrogenase (acceptor), anaerobic glycerol-3-phosphate dehydrogenase, DL-glycerol 3-phosphate oxidase (misleading), FAD-dependent glycerol-3-phosphate dehydrogenase, FAD-dependent sn-glycerol-3-phosphate dehydrogenase, FAD-GPDH, FAD-linked glycerol 3-phosphate dehydrogenase, FAD-linked L-glycerol-3-phosphate dehydrogenase, flavin-linked glycerol-3-phosphate dehydrogenase, flavoprotein-linked L-glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate cytochrome c reductase (misleading), glycerol phosphate dehydrogenase, glycerol phosphate dehydrogenase (acceptor), glycerol phosphate dehydrogenase (FAD), glycerol-3-phosphate CoQ reductase, glycerol-3-phosphate dehydrogenase (flavin-linked), glycerol-3-phosphate:CoQ reductase, glycerophosphate dehydrogenase, L-3-glycerophosphate-ubiquinone oxidoreductase, L-glycerol-3-phosphate dehydrogenase (ambiguous), L-glycerophosphate dehydrogenase, mGPD, mitochondrial glycerol phosphate dehydrogenase, NAD+-independent glycerol phosphate dehydrogenase, pyridine nucleotide- independent L-glycerol 3-phosphate dehydrogenase, sn-glycerol 3-phosphate oxidase (misleading), sn-glycerol-3-phosphate dehydrogenase, sn- glycerol-3-phosphate:(acceptor) 2-oxidoreductase, sn- glycerol-3-phosphate:acceptor 2-oxidoreductase).

Therefore, the bonding between two Ge atoms in digermynes can be described as donor-acceptor interactions using valence bond models. The quartet and doublet structure of RGe fragments It can be seen from the bonding representations that Ge atoms are either linked by one σ-bond and two donor- acceptor bonds (from a filled sp hybrid orbital to an empty p orbital) or one σ-bond and one π-bond with a resonating lone pair or two radicals on each Ge atoms. According to the resonance structures, one of the two Ge atoms bears partial positive charge and is electron deficient, the other Ge atom has an electron lone pair and is able to donate some electron density. Donor-acceptor bonds and resonance structures of digermynes The abnormal bond angles and the single-bond feature of LGeGeL can be rationalized by the electron donating character of N atom, which leads to the formation of N p(π)→Ge (empty p orbital) interaction.

Outer complexes were those in which the intermolecular interaction between the electron donor and acceptor were weak and had very little charge transfer. Inner complexes have extensive charge redistribution. Mulliken’s theory has been used to describe the mechanism by which XB formation occurs.

Schiff bases are common ligands in coordination chemistry. The imine nitrogen is basic and exhibits pi-acceptor properties. The ligands are typically derived from alkyl diamines and aromatic aldehydes. Chiral Schiff bases were one of the first ligands used for asymmetric catalysis.

2.98 Å;Scheiner, S. Ab initio studies of hydrogen bonds: the water dimer paradigm. Annual Review of Physical Chemistry 1994, 45, 23-56. the hydrogen bond is almost linear, but the angle with the plane of the acceptor molecule is about 57°.

TFE forms stable complexes with Lewis bases such as THF or pyridine through hydrogen bonding, yielding 1:1 adducts. CF3CH2OH is classified as a hard Lewis acid and its acceptor properties are discussed in the ECW model yielding EA = 2.07 and CA = 1.06.

The electron flow goes from PSII to cytochrome b6f to PSI. In PSI, the electron gets the energy from another photon. The final electron acceptor is NADP. In oxygenic photosynthesis, the first electron donor is water, creating oxygen as a waste product.

This reaction also shows that manganate(VII) can serve as an electron acceptor in addition to its usual role as an oxygen- transfer reagent. Barium manganate, BaMnO4, is generated by the reduction of KMnO4 with iodide in the presence of barium chloride.

Some of the oxygen atoms in the four OH groups in brazilianite act as donors and some as acceptors of the hydrogen bond. One of these oxygen items is both a donor and acceptor to accommodate the hydrogen that split into two.

Phylloquinone A1 is the next early electron acceptor in PSI. Phylloquinone is also sometimes called vitamin K1. Phylloquinone A1 oxidizes a0 in order to receive the electron and in turn reduces Fx in order to pass the electron to Fb and Fa.

Lee, E.-S. Med. Chem. Lett. 2004, 14, 1333-1337 2-acetylthiophene (46) was treated with iodine and pyridine to generate α-pyridinium acyl ketone 47. Reaction with Michael acceptor 48 under standard conditions yielded functionalized pyridine 49 in 60% overall yield.

This phenomenon gives rise to the wide field of Lewis acid-base chemistry. The driving forces for electron donor and acceptor behavior in chemistry is based on the concepts of electropositivity (for donors) and electronegativity (for acceptors) of atomic or molecular entities.

FRET efficiency can also be determined from the change in the fluorescence lifetime of the donor. The lifetime of the donor will decrease in the presence of the acceptor. Lifetime measurements of the FRET-donor are used in fluorescence-lifetime imaging microscopy (FLIM).

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with a disulfide as acceptor. The systematic name of this enzyme class is (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating).

Germanium(II) hydrides, also called germylene hydrides, are a class of Group 14 compounds consisting of low-valent germanium and a terminal hydride. They are also typically stabilized by an electron donor-acceptor interaction between the germanium atom and a large, bulky ligand.

Unit A represents a 4-chlorophenyl group and unit B a 2,4-dichlorophenyl ring. Unit C is the central pyrazole ring and unit D represents the carbonyl group which serves as the hydrogen bond acceptor. Unit E represents a lipophilic aminopiperidinyl moiety.

It also forms Lewis adducts with group 13 Lewis acids like boron trifluoride.B. Swanson, D. F. Shriver, J. A. Ibers, "Nature of the donor-acceptor bond in acetonitrile-boron trihalides. The structures of the boron trifluoride and boron trichloride complexes of acetonitrile", Inorg. Chem., 2969.

Oxidative protein folding is a process that is responsible for the formation of disulfide bonds between cysteine residues in proteins. The driving force behind this process is a redox reaction, in which electrons pass between several proteins and finally to a terminal electron acceptor.

However, PSCs still suffer from low fill factors (typically below 70%). However, as of 2013, researchers have been able to fabricate PSCs with fill factors of over 75%. Scientists have been able to accomplish via an inverted BHJ and by using nonconventional donor / acceptor combinations.

Devices fabricated using OVPD show a higher short-circuit current density than that of devices made using VTE. An extra layer of donor-acceptor hetero-junction at the top of the cell may block excitons, whilst allowing conduction of electron; resulting in improved cell efficiency.

Conditions for spin coating and evaporation affect device efficiency. Solvent and additives influence donor- acceptor morphology. Additives slow down evaporation, leading to more crystalline polymers and thus improved hole conductivities and efficiencies. Typical additives include 1,8-octanedithiol, ortho-dichlorobenzene, 1,8-diiodooctane (DIO), and nitrobenzene.

Therefore, the donor-acceptor bonds between two Ge atoms are weakened and are more like non-bonding electron lone pairs. It has been suggested that the bond order of Ge-Ge bond is to some degree affected by the electronic properties of bulky protecting groups.

In addition to standard nucleophilic addition reactions on the C=C bond, nitroethylene can serve as a Michael acceptor in a Michael addition reaction. A typical Michael donor (i.e. ketone or aldehyde) can be used.Y. Chi, L. Guo, N. A. Kopf, S. H. Gellman.

Another is known as c.531+5G>C. This mutation destroys the splice acceptor and donor sites resulting in an in-frame deletion. The protein resulting from this gene has a highly altered structure and is not functional. The last is known as c.

In the Mitsunobu reaction, a mixture of triphenylphosphine and diisopropyl azodicarboxylate ("DIAD", or its diethyl analogue, DEAD) converts an alcohol and a carboxylic acid to an ester. The DIAD is reduced as it serves as the hydrogen acceptor, and the PPh3 is oxidized to OPPh3.

Methyl acrylate is a classic Michael acceptor, which means that it adds nucleophiles at its terminus. For example, in the presence of a base catalyst, it adds hydrogen sulfide to give the thioether: :2 CH2CHCO2CH3 \+ H2S → S(CH2CH2CO2CH3)2 It is also a good dienophile.

Studies also show that with upscaling, the PCE in general drops . On all of these areas, NFA- OSCs show great potential but it will take a lot of research before a solid non-fullerene acceptor-organic solar cell can compete with inorganic solar cells.

They are thereby much longer than the ones of GFP derivatives, which are usually between 1,5 and 3 ns. FbFPs are therefore well suited as donor domains in Förster resonance energy transfer (FRET) systems in conjunction with GFP derivatives like YFP as acceptor domains.

In addition, the combination of the donor and acceptor splice junction sequences within short lengths of coding sequence segments that would define exon boundaries would occur rarely in a random sequence. These combined reasons would make introns very long compared to the lengths of exons.

From 1979 to 1990, Kernes worked for a number of enterprises. According to his official biography his career began in 1977. Kernes managed the production and trading company Acceptor from 1992 to 1994. He then became the chairman at CJSC NPK-Holding until 1999.

Martinus Beijerinck discovered the phenomenon of bacterial sulfate reduction, a form of anaerobic respiration. He learned that bacteria could use sulfate as a terminal electron acceptor, instead of oxygen. He isolated and described Spirillum desulfuricans (now called Desulfovibrio desulfuricans), the first known sulfate-reducing bacterium.

The arrangement of materials essentially determines the overall efficiency of the heterojunction solar cell. There are three donor-acceptor bulk morphologies: (a) the bilayer, (b) the bulk heterojunction, and (c) the “comb” structure. Typically, a polymer-fullerene bulk heterojunction solar cell has a layered structure.

Sometimes a dehydrogenase catalyzed reaction will look like this: AH + B+ ↔ A+ \+ BH when a hydride is transferred. Alcohol dehydrogenase oxidizes ethanol, with the help of the electron carrier NAD+, yielding acetaldehydeA represents the substrate that will be oxidized, while B is the hydride acceptor. Note how when the hydride is transferred from A to B, the A has taken on a positive charge; this is because the enzyme has taken two electrons from the substrate in order to reduce the acceptor to BH. The result of a dehydrogenase catalyzed reaction is not always the acquisition of a positive charge. Sometimes the substrate loses a proton.

Aerobic bioremediation is the most common form of oxidative bioremediation process where oxygen is provided as the electron acceptor for oxidation of petroleum, polyaromatic hydrocarbons (PAHs), phenols, and other reduced pollutants. Oxygen is generally the preferred electron acceptor because of the higher energy yield and because oxygen is required for some enzyme systems to initiate the degradation process. Numerous laboratory and field studies have shown that microorganisms can degrade a wide variety of hydrocarbons, including components of gasoline, kerosene, diesel, and jet fuel. Under ideal conditions, the biodegradation rates of the low- to moderate-weight aliphatic, alicyclic, and aromatic compounds can be very high.

Combining the physical and chemical characteristics of conjugated polymers with the high conductivity along the tube axis of carbon nanotubes (CNTs) provides a great deal of incentive to disperse CNTs into the photoactive layer in order to obtain more efficient OPV devices. The interpenetrating bulk donor–acceptor heterojunction in these devices can achieve charge separation and collection because of the existence of a bicontinuous network. Along this network, electrons and holes can travel toward their respective contacts through the electron acceptor and the polymer hole donor. Photovoltaic efficiency enhancement is proposed to be due to the introduction of internal polymer/nanotube junctions within the polymer matrix.

The initial step in this method involves the formation of a silyl ether at the C-2 hydroxy group of the glycosyl donor upon addition of dimethyldichlorosilane in the presence of a strong base such as butyllithium (BuLi); then the glycosyl acceptor is added to form a mixed silaketal. Activation of the anomeric leaving group in the presence of a hindered base then leads to the β-glycoside.Stork, G.; Kim, G. J. Am. Chem. Soc. 1992, 114, 1087-1088 400px A modified silicon-tethering method involves mixing of the glycosyl donor with the glycosyl acceptor and dimethyldichlorosilane in the presence of imidazole to give the mixed silaketal in one pot.

The ABO gene resides on chromosome 9 at the band 9q34.2 and contains 7 exons. The ABO locus encodes three alleles. The A allele produces α-1,3-N-acetylgalactosamine transferase (A-transferase), which catalyzes the transfer of GalNAc residues from the UDP-GalNAc donor nucleotide to the Gal residues of the acceptor H antigen, converting the H antigen into A antigen in A and AB individuals. The B allele encodes α-1,3-galactosyl transferase (B-transferase), which catalyzes the transfer of Gal residues from the UDP-Gal donor nucleotide to the Gal residues of the acceptor H antigen, converting the H antigen into B antigen in B and AB individuals.

5-HT1B and 5-HT1D receptors are considered very similar, they share amino acid homology and their ligands expose similar binding properties thus they have similar pharmacophore. The pharmacophore model for these receptors ligands is qualitative and defines the relative positions of important groups. It is defined with following five main features: an aromatic group (usually the indole), protonated amine (a donor of hydrogen bond), acceptor of hydrogen bond, additional hydrogen bond site (both donor and acceptor) and hydrophobic region located between both hydrogen bond sites, see figure 2. The main binding points were concluded to be the protonated amine and the hydrogen bond site.

Without much doubt, Ser integrases are the current tools of choice for integrating transgenes into a restricted number of well-understood genomic acceptor sites that mostly (but not always) mimic the phage attP site in that they attract an attB-containing donor vector. At this time the most prominent member is PhiC31-INT with proven potential in the context of human and mouse genomes. Contrary to the above Tyr recombinases, PhiC31-INT as such acts in a unidirectional manner, firmly locking in the donor vector at a genomically anchored target. An obvious advantage of this system is that it can rely on unmodified, native attP (acceptor) and attB donor sites.

They can also be produced much more easily via inkjet printing or spray deposition, and therefore are vastly cheaper to manufacture. A downside is that, because they are not crystalline (like silicon), but instead are produced in a purposely disordered blend of electron-acceptor and -donor materials (hence the name bulk heterojunction), they have a limited efficiency of charge transport. However, the efficiencies of these new types of photovoltaic cells have risen from 2.5% in 2001, to 5% in 2006, to greater than 10% in 2011. This is because improved methods for solution processing of acceptor and donor materials led to more efficient blending of the two materials.

The molecule which donates its hydrogen is termed the donor molecule, while the molecule containing lone pair participating in H bonding is termed the acceptor molecule. The number of active pairs is equal to the common number between number of hydrogens the donor has and the number of lone pairs the acceptor has. 200px Though both not depicted in the diagram, water molecules have two active pairs, as the oxygen atom can interact with two hydrogens to form two hydrogen bonds. Intermolecular hydrogen bonding is responsible for the high boiling point of water (100 °C) compared to the other group 16 hydrides, which have little capability to hydrogen bond.

The anabolism of oligosaccharides - and, hence, the role of nucleotide sugars - was not clear until the 1950s when Leloir and his coworkers found that the key enzymes in this process are the glycosyltransferases. These enzymes transfer a glycosyl group from a sugar nucleotide to an acceptor.

This protein complex has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.

Nitrogen fixation also is an important ecological function carried out by some species in this genus, as is growth using molecular hydrogen as a source of energy - neither property are found in every species. Ferric iron can be used by some species as a terminal electron acceptor.

Important variables include materials, solvents and the donor-acceptor weight ratio. The next logical step beyond BHJs are ordered nanomaterials for solar cells, or ordered heterojunctions (OHJs). OHJs minimize the variability associated with BHJs. OHJs are generally hybrids of ordered inorganic materials and organic active regions.

Trafficking protein particle complex subunit 2 is thought to be part of a large multisubunit complex involved in the targeting and fusion of endoplasmic reticulum-to-Golgi transport vesicles with their acceptor compartment. In addition, the encoded protein can bind MBP1 and block its transcriptional repression capability.

Its main products from fermenting fructose or maltose are lactate, acetate, ethanol, glycerol, and carbon dioxide. Lactobacillus pontis cannot use citrate as an electron acceptor in the presence of maltose. There is also no presence of catalase activity. Lactobacillus pontis has the ability to catabolize arginine.

D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 \+ reduced acceptor This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q. D-amino acid dehydrogenase is an enzyme that catalyzes NADPH from NADP+ and D- glucose to produce D- amino acids and glucose dehydrogenase. Some but not limited to these amino acids are D-leucine, D-isoleucine, and D-Valine, which are essential amino acids that humans cannot synthesize due to the fact that they are not included in their diet. Moreover, D- amino acids catalyzes the formation of 2-oxo acids to produce D- amino acids in the presence of DCIP which is an electron acceptor. D-amino acids are used as components of pharmaceutical products, such as antibiotics, anticoagulants, and pesticides, because they have been shown to be not only more potent than their L enantiomers, but also more resistant to enzyme degradation.

The enzymes in this family have amylomaltase or 4-α-glucanotransferase activity () CAZY GH_77, they transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan. They belong to the disproportionating family of enzymes.

In males, the upstream acceptor site is used. This causes a longer version of exon 2 to be included in the processed transcript, including an early stop codon. The resulting mRNA encodes a truncated protein product that is inactive. Females produce the master sex determination protein Sex lethal (Sxl).

H-bond donor ability is classified on a scale (α). Protic solvents can solvate solutes that can accept hydrogen bonds. Similarly, solvents that can accept a hydrogen bond can solvate H-bond-donating solutes. The hydrogen bond acceptor ability of a solvent is classified on a scale (β).

Metal nitrosyls, compounds featuring NO ligands, are numerous. In contrast to metal carbonyls, however, homoleptic metal nitrosyls are rare. NO is a stronger π-acceptor than CO. Well known nitrosyl carbonyls include CoNO(CO)3 and Fe(NO)2(CO)2, which are analogues of Ni(CO)4.

The oxidized reagent forms the colored compound indophenol blue. The cytochrome system is usually only present in aerobic organisms that are capable of using oxygen as the terminal electron acceptor. The end-product of this metabolism is either water or hydrogen peroxide (broken down by catalase).MacFaddin JF, editor.

In comparison to other oxygen-centered oxidants (hypohalites, anions of peroxides) and in line with its low basicity, bromite is a rather weak nucleophile. Rate constants of bromite towards carbocations and acceptor- substituted olefins are by 1–3 orders of magnitude lower than the ones measured with hypobromite.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N-methyl-L-amino- acid:oxygen oxidoreductase (demethylating). Other names in common use include N-methylamino acid oxidase, and demethylase.

The catalytic site of CalG1, CalG3, and CalG4 was shown to possess a highly conserved catalytic dyad of histidine and aspartate which promotes nucleophilic attack on the acceptor hydroxyl group of calicheamicin intermediates. Notably, this motif is absent from CalG2, suggesting a different catalytic mechanism in this enzyme.

Difluorophosphate can form adducts with PF5 and AsF5. In these the oxygen atoms form a donor- acceptor link between the P and As (or P) atoms, linking the difluorides to the pentafluorides. Example salts include KPO2F2·2AsF5, KPO2F2·AsF5, KPO2F2·2PF5 and KPO2F2·PF5. Full article at Eur.

RABAC1 is a gene that in humans encodes the protein Prenylated Rab acceptor 1, also called PRA1, PRAF1, or RABAC1. It is highly conserved in eukaryotes. The protein is localized to Golgi and late endosomes, where it plays a role in vesicular trafficking, lipid transport and cell migration.

Far Red & Near Infrared FUCCI visualizes the birth of a multinucleated cell, which is common in many cancer cells.Kinase FRET sensor. smURFP is a useful acceptor for many red fluorescent proteins due to spectral overlap. A rationally designed red fluorescent protein, stagRFP, allows for easier creation of FRET sensors.

X. azovorans is a chemoorganoheterotroph that carries out oxidative phosphorylation and uses oxygen as a terminal electron acceptor. The organism also has a gene predicted for nitrate reduction. The major quinone isolated was ubiquinone Q-8. This isolation was performed by HPLC methods as described by B.J. Tindall.

Dissimilatory metal-reducing microorganisms are a group of microorganisms (both bacteria and archaea) that can perform anaerobic respiration utilizing a metal as terminal electron acceptor rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration. The most common metals used for this end are iron [Fe(III)] and manganese [Mn(IV)], which are reduced to Fe(II) and Mn(II) respectively, and most microorganisms that reduce Fe(III) can reduce Mn(IV) as well. But other metals and metalloids are also used as terminal electron acceptors, such as vanadium [V(V)], chromium [Cr(VI)], molybdenum [Mo(VI)], cobalt [Co(III)], palladium [Pd(II)], gold [Au(III)], and mercury [Hg(II)].

Desulfovibrio vulgaris is the best-studied sulfate-reducing microorganism species; the bar in the upper right is 0.5 micrometre long. Sulfate-reducing microorganisms (SRM) or sulfate-reducing prokaryotes (SRP) are a group composed of sulfate-reducing bacteria (SRB) and sulfate-reducing archaea (SRA), both of which can perform anaerobic respiration utilizing sulfate (SO42–) as terminal electron acceptor, reducing it to hydrogen sulfide (H2S). Therefore, these sulfidogenic microorganisms "breathe" sulfate rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration. Most sulfate-reducing microorganisms can also reduce some other oxidized inorganic sulfur compounds, such as sulfite (SO32–), dithionite (S2O42–), thiosulfate (S2O32–), trithionate (S3O62–), tetrathionate (S4O62−), elemental sulfur (S8), and polysulfides (Sn2−).

The high time resolution of confocal single-molecule FRET measurements allows to potentially detect dynamics on time scales as low as 10 μs. However, detecting "slow" transitions on timescales longer than the diffusion time (typically ~1 ms), is more difficult than in surface-immobilized experiments and generally requires much longer acquisitions. Normally, the fluorescent emission of both donor and acceptor fluorophores is detected by two independent detectors and the FRET signal is computed from the ratio of intensities in the two channels. Some setup configurations further split each spectral channel (donor or acceptor) in two orthogonal polarizations (therefore requiring 4 detectors) and are able to measure both FRET and fluorescence anisotropy at the same time.

By virtue of their high degree of homology, the new gene copies that came into existence following the gene duplication naturally tend to either unequal crossover or unidirectional gene conversion events. In the latter process, there exists the acceptor and donor sequences and the acceptor sequence will be replaced by a sequence copied from the donor, while the sequence of the donor remains unchanged. The effective homology between the interacting sequences makes the gene conversion event successful. Additionally, the frequency of gene conversion is inversely proportional to the distance between the interacting sequences in cis , and the rate of gene conversion is usually directly proportional to the length of uninterrupted sequence tract in the assumed converted region.

Schematic of energy states in organic solar cells The mechanism of current induction in organic solar cells involves a charge transfer. After electromagnetic absorption and exciton formation in the electron donor polymer, the excited electron is moved towards the acceptor conduction band (LUMO) as a result of the lower energy value than the donor LUMO. This process is called a charge separation, and the corresponding energy value E_{CS} satisfies E_{CS} = E^A_{LUMO} - E^D_{HOMO} where CS denotes charge separation, A denotes the acceptor and D denotes the donor molecule. Along with the Coulombic potential that needs to be surpassed, the maximum energy obtained from the process is defined as the Charge Transfer energy, E_{CT}.

Materials used in polymer-based photovoltaic cells are characterized by their total electron affinities and absorption power. The electron-rich, donor materials tend to be conjugated polymers with relatively high absorption power, whereas the acceptor in this case is a highly symmetric fullerene molecule with a strong affinity for electrons, ensuring sufficient electron mobility between the two. ITO is applied onto glass, and a hole transport layer of PEDOT:PSS (poly(3,4-ethylenedioxythiophene)poly(styrenesulfonate)) on top of that. The photoactive layer is a blend of electron acceptor and donor atoms, and the cathode interlayer is a low work function metal used to lower the work function of the electrode on top to accept electrons.

The final acceptor of this allosteric signal is the catalytic Gly56 within the active site. Inorganic pyrophosphate has 95% the ability of phosphate in inhibiting MGS. 3-phosphoglycerate and phosphoenolpyruvate also have 50% and 70% inhibition, respectively. 2-phosphoglycolate also acts as a competitive inhibitor by mimicking the ene-diolate intermediate.

The word "tawwaab" is said to come from the root t-w-b which has the following classical Arabic connotations: to return; to return to goodness, to repent; to be restored or to be repeatedly summoned or called. The attribute, At Tawwaab, is therefore translated as "The Acceptor of Repentance".

Acrolein is a relatively electrophilic compound and a reactive one, hence its high toxicity. It is a good Michael acceptor, hence its useful reaction with thiols. It forms acetals readily, a prominent one being the spirocycle derived from pentaerythritol, diallylidene pentaerythritol. Acrolein participates in many Diels-Alder reactions, even with itself.

In the dihydrogen bond, however, a metal hydride serves as a proton acceptor, thus forming a hydrogen-hydrogen interaction. Neutron diffraction has shown that the molecular geometry of these complexes is similar to hydrogen bonds, in that the bond length is very adaptable to the metal complex/hydrogen donor system.

Removal of two water molecules gives the compound benzoquinonetetracarboxylic dianhydride, , one of the oxides of carbon. P. R. Hammond (1963), 1,4-Benzoquinone Tetracarboxylic Acid Dianhydride, C10O8: A Strong Acceptor. Science, Vol. 142. no. 3591, p. 502 The acid can be obtained by from durene (1,2,4,5-tetramethylbenzene) via dinitropyromellitic and diaminopyromellitic acids.

It was held that the acceptor was not responsible for any delay in the course of the transit. Hence there was a binding contract. The posting of a letter accepting an offer constitutes a binding contract even if the letter never arrives due to the fault of the post office.

The simplest error cases are the failure of an Acceptor (when a Quorum of Acceptors remains alive) and failure of a redundant Learner. In these cases, the protocol requires no "recovery" (i.e. it still succeeds): no additional rounds or messages are required, as shown below (in the next two diagrams/cases).

Some species of bacteria catalyze redox transformations of arsenic. Dissimilatory arsenate-respiring prokaryotes (DARP) speed up the reduction of As(V) to As(III). DARP use As(V) as the electron acceptor of anaerobic respiration and obtain energy to survive. Other organic and inorganic substances can be oxidized in this process.

In biology, electron donors release an electron during cellular respiration, resulting in the release of energy. Microorganisms, such as bacteria, obtain energy in the electron transfer processes. Through its cellular machinery, the microorganism collects the energy for its use. The final result is the electron is donated to an electron acceptor.

Nitric oxide reductase belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with other acceptors. The systematic name of this enzyme class is nitrous-oxide:acceptor oxidoreductase (NO- forming). Other names in common use include nitrogen oxide reductase, and nitrous-oxide:(acceptor) oxidoreductase (NO-forming).

To do this, a three component system is employed: a catalyst, a photosensitizer and a sacrificial electron acceptor such as persulfate when investigating water oxidation, and a sacrificial electron donor (for example triethylamine) when studying proton reduction. Employing sacrificial reagents in this manner simplifies research and prevents detrimental charge recombination reactions.

A related nitric-oxide reductase () exists in denitrifying species of archaea and eubacteria and is a heterodimer of cytochromes b and c. Phenazine methosulphate can act as acceptor. It has been suggested that cytochrome c oxidase catalytic subunits evolved from ancient nitric oxide reductases that could reduce both nitrogen and oxygen.

Staphylothermus marinus converts sulfur to hydrogen sulfide using these extremozymes. Hydrogen sulfide is then released as a waste product. Staphylothermus marinus contains large protein complexes that are involved in sulfur reduction. Staphylothermus marinus and Staphylothermus hellenicus use sulfur as the final electron acceptor but may use different membrane complexes in sulfur reduction.

In both cases, the acceptor substrate is an asparagine residue. The asparagine residue linked to an N-linked oligosaccharide usually occurs in the sequence Asn-X-Ser/Thr, where X can be any amino acid except for proline, although it is rare to see Asp, Glu, Leu, or Trp in this position.

Phycocyanobilin is a blue phycobilin, i.e., a tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes, and some cryptomonads. Phycocyanobilin is present only in the phycobiliproteins allophycocyanin and phycocyanin, of which it is the terminal acceptor of energy. It is covalently linked to these phycobiliproteins by a thioether bond.

2006, 68, 303. If both the donor and acceptor are sugars, then the product is an oligosaccharide. The reaction requires activation with a suitable activating reagent. The reactions often result in a mixture of products due to the creation of a new stereogenic centre at the anomeric position of the glycosyl donor.

As another consequence of their planar structure and electron-acceptor properties, NDIs intercalate into DNA. Because a range of amines can be condensed with the dianhydride. For example, two useful pigments of the perinone class are generated by condensation with phenylenediamine. A variety of ligands with NDI backbones have also been prepared.

Metal film on top of the organic film applies stresses on the organic film, which helps to prevent the morphological relaxation in the organic film. This gives more densely packed films and at the same time allows the formation of phase-separated interpenetrating donor- acceptor interface inside the bulk of organic thin film.

This enzyme belongs to the family of oxidoreductases, to be specific, those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthine:NAD+ oxidoreductase. Other names in common use include NAD+-xanthine dehydrogenase, xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase.

Some of these enzymes couple phosphotransfer to transmembrane transport. These enzyme/transporters are categorized in the Transporter Classification Database (TCDB) under the Polyphosphate Polymerase/YidH Superfamily (TC# 4.E.1) and are transferases that transfer phosphoyl groups (phosphotransferases) with polyphosphate as the acceptor. The systematic name of this enzyme class is ATP:polyphosphate phosphotransferase.

Denitrification is the utilization of nitrate () as a terminal electron acceptor. It is a widespread process that is used by many members of the Proteobacteria. Many facultative anaerobes use denitrification because nitrate, like oxygen, has a high reduction potential. Many denitrifying bacteria can also use ferric iron () and some organic electron acceptors.

In enzymology, a NAD(P)H dehydrogenase (quinone) () is an enzyme that catalyzes the chemical reaction :NAD(P)H + H+ \+ a quinone \rightleftharpoons NAD(P)+ \+ a hydroquinone The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NAD(P)H:quinone oxidoreductase. Other names in common use include menadione reductase, phylloquinone reductase, quinone reductase, dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,, quinone), DT-diaphorase, flavoprotein NAD(P)H-quinone reductase, menadione oxidoreductase, NAD(P)H dehydrogenase, NAD(P)H menadione reductase, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H: (quinone-acceptor)oxidoreductase, NAD(P)H: menadione oxidoreductase, NADH- menadione reductase, naphthoquinone reductase, p-benzoquinone reductase, reduced NAD(P)H dehydrogenase, viologen accepting pyridine nucleotide oxidoreductase, vitamin K reductase, diaphorase, reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase, vitamin-K reductase, NAD(P)H2 dehydrogenase (quinone), NQO1, QR1, and NAD(P)H:(quinone-acceptor) oxidoreductase.

This characteristic of the recognition between YARS and tRNA(Tyr) has been used to obtain aminoacyl-tRNA synthetases that can specifically charge non-sense suppressor derivatives of tRNA(Tyr) with unnatural aminoacids in vivo without interfering with the normal process of translation in the cell. Both tyrosyl-tRNA synthetases and tryptophanyl-tRNA synthetases belong to Class I of the aminoacyl-tRNA synthetases, both are dimers and both have a class II mode of tRNA recognition, i.e. they interact with their cognate tRNAs from the variable loop and major groove side of the acceptor stem. This is in strong contrast to the other class I enzymes, which are monomeric and approach their cognate tRNA from minor groove side of the acceptor stem.

In enzymology, a D-alanine—alanyl-poly(glycerolphosphate) ligase () is an enzyme that catalyzes the chemical reaction :ATP + D-alanine + alanyl- poly(glycerolphosphate) \rightleftharpoons ADP + phosphate + D-alanyl-alanyl- poly(glycerolphosphate) The 3 substrates of this enzyme are ATP, D-alanine, and alanyl-poly(glycerolphosphate), whereas its 3 products are ADP, phosphate, and D-alanyl-alanyl-poly(glycerolphosphate). This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino- acid ligases (peptide synthases). The systematic name of this enzyme class is D-alanine:alanyl-poly(glycerolphosphate) ligase (ADP-forming). Other names in common use include D-alanyl-alanyl-poly(glycerolphosphate) synthetase, D-alanine:membrane-acceptor ligase, D-alanylalanylpoly(phosphoglycerol) synthetase, D-alanyl-poly(phosphoglycerol) synthetase, and D-alanine-membrane acceptor-ligase.

Specifically, this is the ability to consume simple carbon compounds (energy source) without the presence of an external electron acceptor (such as nitrate or oxygen) by generating energy from internally stored polyphosphate and glycogen. Most other bacteria cannot consume under these conditions and therefore PAOs gain a selective advantage within the mixed microbial community present in the activated sludge. Therefore, wastewater treatment plants that operate for enhanced biological phosphorus removal have an anaerobic tank (where there is no nitrate or oxygen present as external electron acceptor) prior to the other tanks to give PAOs preferential access to the simple carbon compounds in the wastewater that is influent to the plant. A PAO related to the Betaproteobacteria has been identified and named Candidatus Accumulibacter Phosphatis.

In enzymology, a nitrite reductase (NO-forming) () is an enzyme that catalyzes the chemical reaction :nitric oxide + H2O + ferricytochrome c ⇌ nitrite + ferrocytochrome c + 2 H+ The 3 substrates of this enzyme are nitric oxide, H2O, and ferricytochrome c, whereas its 3 products are nitrite, ferrocytochrome c, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor. The systematic name of this enzyme class is nitric-oxide:ferricytochrome-c oxidoreductase. Other names in common use include cd-cytochrome nitrite reductase, [nitrite reductase (cytochrome)] [misleading, see comments.], cytochrome c-551:O2, NO2+ oxidoreductase, cytochrome cd, cytochrome cd1, hydroxylamine (acceptor) reductase, methyl viologen-nitrite reductase, nitrite reductase (cytochrome, and NO-forming).

Further experiments have shown that in this case the transfer occurs not over collisional distances but over the mean intermolecular distances of sensitizer and acceptor, corresponding to a concentration of 10−3 to 10−2M. This is demonstrated by the fact that sensitization occurs with similar half-value concentrations in solution of very different viscosities and even in organic glasses at low temperature. The possibility of the formation of a complex between sensitizer and acceptor molecules was excluded by the additivity of the absorption spectra and the different dependence on concentration to be expected in this case. It must be concluded, therefore, that excitation transfer of a non-trivial nature occurs over the mean distances between statistically distributed molecules which are about 40Å in this case.

Instead, the system was seen to produce hydrogen peroxide, indicating that molecular oxygen acted as a hydrogen acceptor in the system. Bernheim also detected that the enzyme facilitated the occurrence of deamination in tyramine, along with the process of oxidation. Prior to her discovery, tyramine had not been studied extensively from a biochemical perspective.

Phycoerythrobilin is a red phycobilin, i.e. an open tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes and some cryptomonads. Phycoerythrobilin is present in the phycobiliprotein phycoerythrin, of which it is the terminal acceptor of energy. The amount of phycoerythrobilin in phycoerythrins varies a lot, depending on the considered organism.

Subsequent time resolved detection of the metal-centered luminescent probe yields the desired signal. Antigens, steroids and hormones are routinely assayed with heterogeneous techniques. Homogeneous assays rely on direct coupling of the lanthanide label with an organic acceptor. The relaxation of excited molecules states often occurs by the emission of light which is called fluorescence.

The distinctive coloring has led to coining the term 'little blue box' for cyclophane, an important π-acceptor used to synthesize mechanically bonded structures. Stoddart maintains this standardized color scheme across all of his publications and presentations, and his style has been adopted by other researchers reporting mechanically interlocked molecules based on his syntheses.

Mechanism for the hydrogenation of an alkene catalyzed by the homogeneous catalyst Wilkinson's catalyst. ;Hydrogenation and related reactions A prominent class of reductive transformations are hydrogenations. In this process, H2 added to unsaturated substrates. A related methodology, transfer hydrogenation, involves by transfer of hydrogen from one substrate (the hydrogen donor) to another (the hydrogen acceptor).

Chlorophyll a is very important in the energy phase of photosynthesis. Two electrons need to be passed to an electron acceptor for the process of photosynthesis to proceed. Within the reaction centers of both photosystems there are a pair of chlorophyll a molecules that pass electrons on to the transport chain through redox reactions.

The unstable 14-electron Cp2ZrII-compound is generally non- existent, but can be generated using ligands that stabilize the metallocene fragment. Optimally, these ligands can be quantitatively released under mild conditions. One option is the usage of π-acceptor ligands like carbon monoxide. Furthermore, a reaction with trimethylphosphine yields Cp2ZrII- complex as illustrated below.

The inserted sequence is flanked by two introns marked with GT/AG donor-acceptor sites that are necessary for U2-dependent splicing. Consequently, incorporation or bypass of exon14a results in the short or long isoforms, respectively. It is suggested that efficient splicing of the exon14a segment necessitates the specialized environment of TG in vampire bats.

Since the fluorescence lifetime of a fluorophore depends on both radiative (i.e. fluorescence) and non-radiative (i.e. quenching, FRET) processes, energy transfer from the donor molecule to the acceptor molecule will decrease the lifetime of the donor. Thus, FRET measurements using FLIM can provide a method to discriminate between the states/environments of the fluorophore.

Bulk heterojunctions (BHJs) address this shortcoming. In a BHJ, a blend of electron donor and acceptor materials is cast as a mixture, which then phase-separates. Regions of each material in the device are separated by only several nanometers, a distance suited for carrier diffusion. BHJs require sensitive control over materials morphology on the nanoscale.

This protein complex has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2.

Venenivibrio stagnispumantis displays tolerance to relatively high concentrations of arsenic and antimony compounds. Cells grew in the presence of up to 8 mM arsenite (As3+), 15 mM trivalent antimony (Sb3+), and >20 mM arsenate (As5+) but growth was not observed when As3+ and As5+ were provided as the sole electron donor and acceptor pair.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is 2-hydroxy-1,4-benzoquinone:NADH oxidoreductase. Other names in common use include hydroxybenzoquinone reductase, 1,2,4-trihydroxybenzene:NAD oxidoreductase, and NADH:2-hydroxy-1,4-benzoquinone oxidoreductase.

With a pKa of 5.25 for its conjugate acid, pyridine is about 15x less basic than imidazole. Pyridine is a weak pi-acceptor ligand. Trends in the M-N distances for complexes of the type [MCl2(py)4]2+ reveal an anticorrelation with d-electron count. Few low-valent metal complexes of pyridines are known.

Thereby, most sv-LAAOs are considered to be thermolabile enzymes. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-amino- acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio- amino-acid oxidase.

Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases. Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry of the resulting products. Examples of trans-prenyltranferases include dimethylallyltranstransferase, and geranylgeranyl pyrophosphate synthase.

For example, glycine with two carbons is converted to acetate. In this way, amino acid fermenting microbes can avoid using hydrogen ions as electron acceptors to produce hydrogen gas. Amino acids can be Stickland acceptors, Stickland donors, or act as both donor and acceptor. Only histidine cannot be fermented by Stickland reactions, and is oxidised.

Further studies of the Hill reaction were made in 1957 by plant physiologist Daniel I. Arnon. Arnon studied the Hill reaction using a natural electron acceptor, NADP. He demonstrated the light-independent reaction, observing the reaction under dark conditions with an abundance of carbon dioxide. He found that carbon fixation was independent of light.

Nagios Remote Data Processor (NRDP) is a Nagios agent with a flexible data transport mechanism and processor. It is designed with an architecture that allows it to be easily extended and customized. NRDP uses standard ports and protocols (HTTP and XML) and can be implemented as a replacement for Nagios Service Check Acceptor (NSCA).

The hydrogenation of a methenyl-H4MPT+ occurs instead of H2 oxidation/production, which is the case for the other two types of hydrogenases. While the exact mechanism of the catalysis is still under study, recent finding suggests that molecular hydrogen is first heterolytically cleaved by Fe(II), followed by transfer of hydride to the carbocation of the acceptor.

5.1 hydrogen:quinone oxidoreductase : H2 \+ menaquinone menaquinol ;EC 1.12.7.2 ferredoxin hydrogenase (hydrogen:ferredoxin oxidoreductase) : H2 \+ oxidized ferredoxin 2H+ \+ reduced ferredoxin ;EC 1.12.98.1 coenzyme F420 hydrogenase (hydrogen:coenzyme F420 oxidoreductase) : H2 \+ coenzyme F420 reduced coenzyme F420 ;EC 1.12.99.6 hydrogenase (acceptor) (hydrogen:acceptor oxidoreductase) : H2 \+ A AH2 ;EC 1.12.98.2 5,10-methenyltetrahydromethanopterin hydrogenase (hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase) : H2 \+ 5,10-methenyltetrahydromethanopterin H+ \+ 5,10-methylenetetrahydromethanopterin ;EC 1.12.

If we assume full ionization and that n, p \ll N_D, N_A , then: :::qN_Aw_P \approx qN_Dw_N \,. where w_P and w_N are depletion widths in the p and n semiconductor, respectively. This condition ensures that the net negative acceptor charge exactly balances the net positive donor charge. The total depletion width in this case is the sum w =w_N +w_P.

During this stage, the state of hypoperfusion causes hypoxia. Due to the lack of oxygen, the cells perform lactic acid fermentation. Since oxygen, the terminal electron acceptor in the electron transport chain, is not abundant, this slows down entry of pyruvate into the Krebs cycle, resulting in its accumulation. The accumulating pyruvate is converted to lactate by lactate dehydrogenase.

History of ssrA. Precursor RNAs are shown, whose dashed portions are excised during maturation. The permuted genes produce both an acceptor piece (red) and coding piece (blue); dotted lines mark secondary structures not always present. Abbreviations: TLD, tRNA- like domain; MLR, mRNA-like region; ITS, internal transcribed spacer; P, paired region; PK, pseudoknot; RF, reading frame.

This is an example of exon skipping. The intron upstream from exon 4 has a polypyrimidine tract that doesn't match the consensus sequence well, so that U2AF proteins bind poorly to it without assistance from splicing activators. This 3' splice acceptor site is therefore not used in males. Females, however, produce the splicing activator Transformer (Tra) (see below).

Obligate anaerobes metabolise energy by anaerobic respiration or fermentation. In aerobic respiration, the pyruvate generated from glycolysis is converted to acetyl-CoA. This is then broken down via the TCA cycle and electron transport chain. Anaerobic respiration differs from aerobic respiration in that it uses an electron acceptor other than oxygen in the electron transport chain.

In order to work as a catalyst, GOx requires a cofactor, flavin adenine dinucleotide (FAD). FAD is a common component in biological oxidation-reduction (redox reactions). Redox reactions involve a gain or loss of electrons from a molecule. In the GOx-catalyzed redox reaction, FAD works as the initial electron acceptor and is reduced to FADH2.

Rauhut-Currier reaction is a reaction of activated alkene and a Michael acceptor, not an aldehyde or an imine. It is also called a vinylogous MBH reaction. Because Rauhut-Currier reaction often couple two activated alkenes, there have been problems with selectivity. Intramolecular Rauhut-Currier reaction has been employed by the virtue of improved reactivity and selectivity.

GeSbTe is generally p type and there are many electronic states in the band gap accounting for acceptor and donor like traps. GeSbTe has two stable states, crystalline and amorphous. The phase change mechanism from high resistance amorphous phase to low resistance crystalline phase in nano-timescale and threshold switching are two of the most important characteristic of GeSbTe.

It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.

Voet, D, Voet, J. G., Biochemistry (3rd Edition), John Wiley & Sons, Inc., 2004, pg 1095 GMP is formed by the inosinate oxidation to xanthylate (XMP), and afterwards adds an amino group on carbon 2. Hydrogen acceptor on inosinate oxidation is NAD+. Finally, carbon 2 gains the amino group by spending an ATP molecule (which becomes AMP+2Pi).

At the kinase domain it exhibits about 70% similarity with the ERK4 protein. The activation loop of the phosphorylation motif contains only one phospho acceptor site (Ser-Glu-Gly). The structure is predicted by homology modelling using the crystal structure of phoshphorylated ERK2. According to the model, the structure of ERK3/MAPK6 kinase domain resembles other MAP kinases.

Palaeococcus ferrophilus is a barophilic, hyperthermophilic archaeon from a deep-sea hydrothermal vent chimney. It cells are irregular cocci and motile with multiple polar flagella. Paleococcus was the third genus within Euryarchaeota to be described in the literature. These organisms prefer to use elemental sulfur as an electron acceptor, but they can also use ferrous oxide.

Redox reactions are preferably run in polar solvents. Donor and acceptor then have a solvent shell and the precursor and successor complexes are solvated also. The closest molecules of the solvent shell, or the ligands in complexes, are tightly bound and constitute the "inner sphere". Reactions in which these participate are called inner sphere redox reactions.

Before sulfate can be used as an electron acceptor, it must be activated. This is done by the enzyme ATP-sulfurylase, which uses ATP and sulfate to create adenosine 5'-phosphosulfate (APS). APS is subsequently reduced to sulfite and AMP. Sulfite is then further reduced to sulfide, while AMP is turned into ADP using another molecule of ATP.

Dimethyl acetylenedicarboxylate (DMAD) is an organic compound with the formula CH3O2CC2CO2CH3. It is a di-ester in which the ester groups are conjugated with a C-C triple bond. As such, the molecule is highly electrophilic, and is widely employed as a dienophile in cycloaddition reactions, such as the Diels- Alder reaction. It is also a potent Michael acceptor.

The glycosyl donor is protected at C-2 by OAll group. The allyl group is then isomerized to a prop-1-enyl ether using a rhodium hydride generated from Wilkinson's catalyst ((PPh3)3RhCl) and butyllithium (BuLi). The resulting enol ether is then treated with NIS and the glycosyl acceptor to generate a mixed acetal. The 1,2-cis (e.g.

Type I photosystems use ferredoxin-like iron-sulfur cluster proteins as terminal electron acceptors, while type II photosystems ultimately shuttle electrons to a quinone terminal electron acceptor. Both reaction center types are present in chloroplasts and cyanobacteria, and work together to form a unique photosynthetic chain able to extract electrons from water, creating oxygen as a byproduct.

Pseudomonas fluorescens has multiple flagella. It has an extremely versatile metabolism, and can be found in the soil and in water. It is an obligate aerobe, but certain strains are capable of using nitrate instead of oxygen as a final electron acceptor during cellular respiration. Optimal temperatures for growth of P. fluorescens are 25–30°C.

Sulfate reduction, which occurs with the help of sulfate-reducing microorganisms, is used in the cryptic sulfur cycle. This cycle is continuous oxidation and reduction of sulfate and uses sulfate as the terminal electron acceptor rather than oxygen. The cycle was purposed to help contribute to the energy flow to anoxic water off the coast of Chile.

The sugar-phosphate backbone has multiplex electronic structure and the electron delocalisation complicates its theoretical description. Some part of the electronic density is delocalised over the whole backbone and the extent of the delocalisation is affected by backbone conformation due to hyper- conjugation effects. Hyper-conjugation arises from donor-acceptor interactions of localised orbitals in 1,3 positions.

Methylene chloride is a Lewis acid that can hydrogen bond to electron donors. It is classified as a hard acid and is included in the ECW model. It is a solvent that has been used in many thermodynamic studies of donor-acceptor bonding. The donor hydrogen-bonding corrections of methylene chloride in these thermodynamic studies has been reported.

Denitrification is the reduction of nitrates back into nitrogen gas (N2), completing the nitrogen cycle. This process is performed by bacterial species such as Pseudomonas and Paracoccus, under anaerobic conditions. They use the nitrate as an electron acceptor in the place of oxygen during respiration. These facultatively (meaning optionally) anaerobic bacteria can also live in aerobic conditions.

An example of such a reaction is methane oxidation: :CH4 \+ O2 → CO2 \+ 2 H2O Here CH4 is the donor and O2 is the acceptor. Donors can be considered "edibles" and acceptors "breathables". The amount of energy that is released in a metabolic reaction depends on the redox potential of the chemicals involved. Electron donors have negative potentials.

The cellular retinaldehyde-binding protein transports 11-cis- retinal (also known as 11-cis-retinaldehyde) as its physiological ligands. It plays a critical role as an 11-cis-retinal acceptor which facilitates the enzymatic isomerization of all 11-trans-retinal to 11-cis-retinal, in the isomerization of the rod and cones of the visual cycle.

The colorless cells are disk-shaped or cylindrical, arranged in long filaments with a cell diameter that can measure between 12 and 160 micrometres (different subspecies). A massive central vacuole is used for accumulation of nitrate, presumably for use as an electron acceptor in anaerobic sulfide oxidation. The filaments are surrounded by slime and can move by gliding.

Another consequence is that they are easily coupled to compatible donor polymers. However, fullerene acceptor organic solar cells (FA-OSCs) encounter a limited efficiency. The energy levels in fullerene compounds are relatively constant and difficult to alter. Moreover, they employ weak absorption in the visible spectrum and the near-infrared spectrum and low thermal instability and photochemical instability.

Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase (GT). In other words, it transfers glucose from uridine diphospho-glucose (UDPglucose) to an acceptor, modified DNA through beta-Glycosidic bond. The role of the enzyme is to protect the infecting viral DNA from the bacteria's restriction enzymes. Glucosylation prevents the virus DNA from being cut up.

The microorganism attempt to maximize their energy gain by selecting the electron acceptor with the highest potential available. In nature mainly minerals containing iron or manganese oxides are being reduced. Often soluble electron acceptors are depleted in the microbial environment. The microorganism can also maximize their energy selecting a good electron donor which can be easily metabolized.

These processes are done by extracellular electron transfer (EET). The theoretical energy gain ΔG for microorganisms relates directly the potential difference between the electron acceptor and the donor. But the inefficiencies like internal resistances will decrease this energy gain. The advantage of these devices is their high selectivity and in high speed processes limited by kinetic factors.

Grx2 functions as a part of the cellular redox signaling pathway and antioxidant defense mechanism. As a GRX family protein, Grx2 acts as an electron donor to deglutathionylate proteins. It has also been shown to reduce both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal. Grx2 is also an electron acceptor.

Its relative acceptor strength toward a series of bases, versus other Lewis acids, can be illustrated by C-B plots.Laurence, C. and Gal, J-F. Lewis Basicity and Affinity Scales, Data and Measurement, (Wiley 2010) pp 50-51 IBSN 978-0-470-74957-9Cramer, R. E., and Bopp, T. T. (1977) Great E and C plot.

In enzymology, a D-alanine—poly(phosphoribitol) ligase () is an enzyme that catalyzes the chemical reaction :ATP + D-alanine + poly(ribitol phosphate) \rightleftharpoons AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate) The 3 substrates of this enzyme are ATP, D-alanine, and poly(ribitol phosphate), whereas its 3 products are AMP, diphosphate, and O-D-alanyl-poly(ribitol phosphate). This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is D-alanine:poly(phosphoribitol) ligase (AMP-forming). Other names in common use include D-alanyl-poly(phosphoribitol) synthetase, D-alanine: membrane acceptor ligase, D-alanine-D-alanyl carrier protein ligase, D-alanine-membrane acceptor ligase, and D-alanine-activating enzyme.

More recently a Pd-catalyzed cyclopentannulation followed by Scholl cyclodehydrogenation devised by Kyle Plunkett's research group has been found valuable for synthesizing the five-membered ring core poly aromatic contorted molecules. Based on the hypothesis that the five membered cyclopentaaceanthralene core is a part of the fullerene itself and can help assist conjugation in the molecule in its substituted form. Fig.10: C60 and C70 with their scaffolds used to develop contorted PAHs The resonance structures Figure 10 show that the five-membered aromatic ring core can accept a pair of electrons in one of its (anti aromatic) resonance structures to afford cyclopentadienyl anion (aromatic) rings and thus can behave as a good electron acceptor molecule. The tendency to achieve low energy aromatic structure makes it a good electron acceptor core.

An extrinsic semiconductor which has been doped with electron donor atoms is called an n-type semiconductor, because the majority of charge carriers in the crystal are negative electrons. An electron acceptor dopant is an atom which accepts an electron from the lattice, creating a vacancy where an electron should be called a hole which can move through the crystal like a positively charged particle. An extrinsic semiconductor which has been doped with electron acceptor atoms is called a p-type semiconductor, because the majority of charge carriers in the crystal are positive holes. Doping is the key to the extraordinarily wide range of electrical behavior that semiconductors can exhibit, and extrinsic semiconductors are used to make semiconductor electronic devices such as diodes, transistors, integrated circuits, semiconductor lasers, LEDs, and photovoltaic cells.

In molecular biology, the octopine dehydrogenase family of enzymes act on the CH-NH substrate bond using NAD(+) or NADP(+) as an acceptor. The family includes octopine dehydrogenase , nopaline dehydrogenase , lysopine dehydrogenase and opine dehydrogenase . NADPH is the preferred cofactor, but NADH is also used. Octopine dehydrogenase is involved in the reductive condensation of arginine and pyruvic acid to D-octopine.

Phycourobilin is an orange tetrapyrrole involved in photosynthesis in cyanobacteria and red algae. This chromophore is bound to the phycobiliprotein phycoerythrin, the distal component of the light-harvesting system of cyanobacteria and red algae (phycobilisome). When bound to phycoerythrin, phycourobilin shows an absorption maximum around 495 nm. This chromophore is always a donor chromophore of phycoerythrins, since their acceptor chromophore is always phycoerythrobilin.

Ionized manganese is used industrially as pigments of various colors, which depend on the oxidation state of the ions. The permanganates of alkali and alkaline earth metals are powerful oxidizers. Manganese dioxide is used as the cathode (electron acceptor) material in zinc- carbon and alkaline batteries. In biology, manganese(II) ions function as cofactors for a large variety of enzymes with many functions.

It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2.

After oxygen, nitrate, manganeses, and iron are depleted, sulfate is the main electron acceptor used in anaerobic respiration. The metabolism associated with this is dissimilatory sulfate reduction (DSR) and is carried out by sulfur-reducing bacteria, which are widely distributed in anoxic environments. DSR oxidizes organic carbon using sulfate, and is described by the following equation: SO4^2- +2CH2O -> H2S +2HCO3^-.

It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2.

The rule usefully predicts the formulas for low-spin complexes of the Cr, Mn, Fe, and Co triads. Well- known examples include ferrocene, iron pentacarbonyl, chromium carbonyl, and nickel carbonyl. Ligands in a complex determine the applicability of the 18-electron rule. In general, complexes that obey the rule are composed at least partly of π-acceptor ligands (also known as π-acids).

Jeffries-EL served as a Martin Luther King visiting professor at Massachusetts Institute of Technology between 2014 and 2015. Here, her group focused on the synthesis of polymer building blocks, including heterocyclic electron-rich (donor) and electron-poor (acceptor) units. For electron-deficient units, Jeffries-EL develops benzobisazoles. She is interested in cross-conjugated organic semiconductors, including benzodifurans, as well as functional Polythiophenes.

Labels are identifiers followed by a colon (':'). At the root, Joule is an imperative language and because of that a statement-based language. It has a rich expression syntax, which transforms easily to its relational syntax underneath. Complex expressions become separate statements, where the site of the original expression is replaced by a reference to the acceptor of the results channel.

The reactivity of picryl chloride is strongly influenced by the presence of three electron-withdrawing nitro groups. Consequently picryl chloride is an electrophile as illustrated by its reactivity toward sulfite to give the sulfonate: :ClC6H2(NO2)3 \+ Na2SO3 → NaO3SC6H2(NO2)3 \+ NaCl Picryl chloride is also a strong electron acceptor. It forms a 1:1 charge-transfer complex with hexamethylbenzene.

Stryer and coworkers pioneered the use of fluorescence spectroscopy, particularly Förster resonance energy transfer (FRET), to monitor the structure and dynamics of biological macromolecules. In 1967, Stryer and Haugland showed that the efficiency of energy transfer depends on the inverse sixth power of the distance between the donor and acceptor,Lakowicz, J.R., 2006. Principles of Fluorescence Spectroscopy (Springer, 3rd ed., p.

Efficient photogeneration can only occur in binary systems due to charge transfer between donor and acceptor moieties. Otherwise neutral excitons decay radiatively to the ground state – thereby emitting photoluminescence – or non- radiatively. The optical absorption edge of organic semiconductors is typically 1.7–3 eV, equivalent to a spectral range from 700 to 400 nm (which corresponds to the visible spectrum).

196delC, a heterozygous mutation leading to a frameshift in exon 3, c.41-2A>G, a heterozygous splice mutation in a novel acceptor site in intron 1, and c.55C>T, a heterozygous nonsense mutation in exon 2. Additionally, experiments with Oryzias latices suggest COX7B may be associated with microphthalmia with linear skin lesions (MLS), an X-linked, dominant, male-lethal mitochondrial disorder.

In many metabolic reactions, a protein that acts as an electron carrier binds to an enzyme that acts its reductase. After it receives an electron, it dissociates and then binds to the next enzyme that acts its oxidase (i.e. an acceptor of the electron). These interactions between proteins are dependent on highly specific binding between proteins to ensure efficient electron transfer.

The average distance an exciton can diffuse through a material before annihilation by recombination is the exciton diffusion length. This is short in polymers, on the order of 5–10 nanometers. The time scale for radiative and non-radiative decay is from 1 picosecond to 1 nanosecond. Excitons generated within this length close to an acceptor would contribute to the photocurrent.

Mackenzie, L. F.; Wang, Q.; Warren, R. A. J.; Withers, S. G. J. Am. Chem. Soc. 1998, 120, 5583-5584 When incubated with α-glycosyl fluorides and an acceptor sugar it was found to catalyze the transglycosidation reaction without any hydrolysis. This glycosynthase was used to synthesize a series of di- and trisaccharide products with yields between 64% and 92%.

However, there are several caveats to be aware of when interpreting data produced using bicistronic reporter constructs. For example, there are several known cases of mis-reported IRES elements that were later recognized as promoter-containing regions. More recently, splice acceptor sites within several presumed IRES segments have been shown to be responsible for apparent IRES function in bicistronic reporter assays.

Phycoerythrobilin is present in the phycobiliprotein phycoerythrin, the terminal acceptor of energy during the process of photosynthesis. The phycoerythrin was translocated into the thylakoid lumen with its chromophore composition altered; subsequently, phycobiliproteins with at least seven different absorption spectra evolved. Cryptomonas is distinguished by the purple phycoerythrin 566 as an accessory pigment, which gives the organisms a brownish color in appearance.

The acid is referred to as a proton donor and the base as a proton acceptor. Likewise, biochemical terms such as proton pump and proton channel refer to the movement of hydrated ions. The ion produced by removing the electron from a deuterium atom is known as a deuteron, not a proton. Likewise, removing an electron from a tritium atom produces a triton.

Aerobic respiration, in which oxygen is used as the terminal electron acceptor, is crucial to all water-breathing fish. When fish are deprived of oxygen, they require other ways to produce ATP. Thus, a switch from aerobic metabolism to anaerobic metabolism occurs at the onset of hypoxia. Glycolysis and substrate-level phosphorylation are used as alternative pathways for ATP production.

Other trivalent dopants include indium (In) and gallium (Ga). When substituting for a Si atom in the crystal lattice, the three valence electrons of boron form covalent bonds with three of the Si neighbours but the bond with the fourth neighbour remains unsatisfied. The initially electro-neutral acceptor becomes negatively charged (ionised). The unsatisfied bond attracts electrons from the neighbouring bonds.

The antenna complex with energy transfer within the thylakoid membrane of a chloroplast. Chlorophyll a in the reaction center is the only pigment to pass boosted electrons to an acceptor (modified from 2). Absorption of light by photosynthetic pigments converts photons into chemical energy. Light energy radiating onto the chloroplast strikes the pigments in the thylakoid membrane and excites their electrons.

Dehalogenimonas lykanthroporepellens is a chemotrophic organism that uses H2 as an electron donor and polychlorinated aliphatic alkanes as an electron acceptor. These molecules include 1,2,3-trichloropropane, 1,2-dichloropropane, 1,1,2,2-tetrachloroethane, 1,1,2-trichloroethane, and 1,2-dichloroethane. However, there are several chlorinated alkanes that it cannot reduce, such as 1-chloropropane and 2-chloropropane. It uses these compounds as electron acceptors in dihaloelimination reactions.

RNA polymerase from Saccharomyces cerevisiae complexed with α-amanitin (in red). Despite the use of the term "polymerase," RNA polymerases are classified as a form of nucleotidyl transferase. A transferase is any one of a class of enzymes that enact the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor).

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include hydroxyphenylpyruvate synthase, and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+ oxidoreductase. Another name in common use is (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase. This enzyme employs one cofactor, iron.

For instance, phosgene is a highly reactive nucleophile acceptor, which makes it an excellent reagent for polymerizing diols and diamines to produce polycarbonate and polyurethane plastics. For this use, millions of tons are produced annually. However, the same reactivity makes it also highly reactive towards proteins in human tissue and thus highly toxic. In fact, phosgene has been used as a chemical weapon.

Thus, the two substrates of this enzyme are L-glutamate and NAD+, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in glutamate metabolism and nitrogen assimilation. It employs one cofactor, FMN.

This enzyme belongs to the family of oxidoreductases, to be specific those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is [methionine synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+ oxidoreductase. Other names in common use include methionine synthase cob(II)alamin reductase (methylating), methionine synthase reductase, [methionine synthase]-cobalamin methyltransferase (cob(II)alamin, and reducing).

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming). Other names in common use include 5-N-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase, and (L-ornithine- forming).

In , the manganese atoms provide a magnetic moment, and each also acts as an acceptor, making it a p-type material. The presence of carriers allows the material to be used for spin-polarized currents. In contrast, many other ferromagnetic magnetic semiconductors are strongly insulating and so do not possess free carriers. is therefore a candidate as a spintronic material.

Early in his career, Henry identified the source of red light emission in gallium phosphide LEDs. In 1968, he and coworkers reported that the red luminescence originated from an electron-hole pair bound to a nearest neighbor donor-acceptor pair composed of zinc and oxygen.C.H. Henry, P.J. Dean, and J.D. Cuthbert, "New Red Pair Luminescence From GaP," Phys. Rev. 166, 754 (1968).

Beijerinck discovered the phenomenon of bacterial sulfate reduction, a form of anaerobic respiration. He learned bacteria could use sulfate as a terminal electron acceptor, instead of oxygen. This discovery has had an important impact on our current understanding of biogeochemical cycles. Spirillum desulfuricans, now known as Desulfovibrio desulfuricans, the first known sulfate-reducing bacterium, was isolated and described by Beijerinck.

The cylindrical assemblies possess internal helical order and self- organize into columnar liquid crystalline lattices. When inserted into vesicular membranes, the porous cylindrical assemblies mediate transport of protons across the membrane. Self-assembly of dendrons generates arrays of nanowires. Electron donor-acceptor complexes comprise the core of the cylindrical supramolecular assemblies, which further self-organize into two- dimensional columnar liquid crystaline lattices.

Vitamin K1 is an important chemical in green plants, where it functions as an electron acceptor in photosystem I during photosynthesis. For this reason, vitamin K1 is found in large quantities in the photosynthetic tissues of plants (green leaves, and dark green leafy vegetables such as romaine lettuce, kale, and spinach), but it occurs in far smaller quantities in other plant tissues.

Glutaryl-CoA dehydrogenase (GCDH) is an enzyme encoded by the GCDH gene on chromosome 19. The protein belongs to the acyl-CoA dehydrogenase family (ACD). It catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor.

The electron transport chain is built up of peptides, enzymes, and other molecules. The flow of electrons through the electron transport chain an exergonic process. The energy from the redox reactions create an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of electrons terminates with molecular oxygen being the final electron acceptor.

APH(3') is primarily found in certain species of gram-positive bacteria. APH(3') catalyzes the phosphorylation of kanamycin A, a 4,6-disubstituted aminoglycoside, at the 3'-hydroxyl group. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:kanamycin 3'-O-phosphotransferase.

In this context, a Group V element is said to behave as an electron donor, and a group III element as an acceptor. This is a key concept in the physics of a diode. A very heavily doped semiconductor behaves more like a good conductor (metal) and thus exhibits more linear positive thermal coefficient. Such effect is used for instance in sensistors.

Through their haemoglobin- degrading activity, they are an important cause of symptoms in malaria sufferers. Consequently, this family of enzymes is a potential target for antimalarial drugs. Plasmepsins are aspartic acid proteases, meaning their active site contains two aspartic acid residues. These two aspartic acid residue act respectively as proton donor and proton acceptor, catalysing the hydrolysis of peptide bond in proteins.

Cynaropicrin shows a reduction in parasitemia in murine models and has potent antitrypanosomal activity. It lowers intracellular GSH and trypanothione levels and inhibits trypanosomal ornithine decarboxylase with its α,β-unsaturated methylene moiety which acts as Michael acceptor. This leads to apoptosis of parasites. The 2-hydroxymethyl-2-propenoyl moiety was found to play an important role in the toxicity.

Scheme 13. Asymmetric Intermolecular Stetter Reaction with Nitroalkenes Another contribution to the development of asymmetric intermolecular Stetter reactions came from Glorius and coworkers in 2011. They demonstrated the synthesis of α-amino acids enantioselectively by utilizing N-acylamido acrylate as the conjugate acceptor. Significantly, the reaction can be run on a 5 mmol scale without loss of yield or enantioselectivity.

CDO is responsible for the first major step in metabolism of cysteine. CDO oxidizes to cysteine sulfinic acid (which exists predominantly in the anionic sulfinate form in vivo). Overall, CDO catalyzes the addition of dioxygen (O2) to a thiol, producing a sulfinic acid. More specifically, CDO is part of the group of non-heme iron oxygenases that employ oxygen as an electron acceptor.

Collison is regarded one of the leading researchers in electron paramagnetic resonance spectroscopy . For his significant contributions to the experimental and theoretical fundamentals of transition metal electron paramagnetic resonance, from bioinorganic chemistry to molecular materials, and for his contribution to the book Electron Paramagnetic Resonance (Volume 19), he received the Bruker Prize in 2020, which is one of the world's highest awards in electron paramagnetic resonance. In 2016, Collison participated in a research which reported the use of an organic donor–acceptor polymer containing a viologen electron acceptor and triarylamine electron donor as a platform in the development of multifunctional materials. The research explored the interplay between electronic and host–guest interactions in the synthesized polymers; POP-V1 containing a redox active triarylamine core and POP-V2 containing a redox inactive benzene core, in which the redox states present can be reversibly accessed.

In this example, the β-carbon of the α,β-unsaturated ester 1 formally acts as a nucleophile, whereas normally it would be expected to be a Michael acceptor. Scheme 3. Umpolung of Michael Acceptors This carbene reacts with the α,β-unsaturated ester 1 at the β-position forming the intermediate enolate 2. Through tautomerization 2b can displace the terminal bromine atom to 3.

To test this, a quick oxidase test for cytochrome c oxidase is performed. Enterobacteriaceae are typically oxidase negative, meaning they either do not use oxygen as an electron acceptor in the electron transport chain, or they use a different cytochrome enzyme for transferring electrons to oxygen. If the culture is determined to be oxidase positive, alternative tests must be carried out to correctly identify the bacterial species.

The overall process of glycolysis is: :Glucose + 2 NAD+ \+ 2 ADP + 2 Pi → 2 pyruvate + 2 NADH + 2 H+ \+ 2 ATP If glycolysis were to continue indefinitely, all of the NAD+ would be used up, and glycolysis would stop. To allow glycolysis to continue, organisms must be able to oxidize NADH back to NAD+. How this is performed depends on which external electron acceptor is available.

Chloranil is produced by chlorination of phenol to give hexachlorocyclohexa-2,5-dien-1-one ("hexachlorophenol"). Hydrolysis of the dichloromethylene group in this dienone gives chloranil:François Muller and Liliane Caillard "Chlorophenols" in Ullmann's Encyclopedia of Industrial Chemistry Wiley-VCH, Weinheim, 2011. :C6H5OH + 6 Cl2 → C6Cl6O + 6 HCl :C6Cl6O + H2O → C6Cl4O2 \+ 2 HCl Chloroanil serves as a hydrogen acceptor. It is more electrophilic than quinone itself.

Measurements of production of singlet oxygen by photoinhibited PSII provided further evidence for an acceptor-side-type mechanism. The concept of a repair cycle that continuously repairs photoinhibitory damage, evolved and was reviewed by Aro et al. in 1993. Many details of the repair cycle, including the finding that the FtsH protease plays an important role in the degradation of the D1 protein, have been discovered since.

After Naoto saved him from Kahn, Takeshi developed Grid Hyper Beam, which was used to decimate both Kahn and his home's computer. 22 years later in the event anime Denkou Choujin Gridman: boys invent great heroes, Takeshi bonds with Gridman Sigma, transforming with the Acceptor to fight against real life monsters. Takeshi Todo is portrayed by and is voiced by in the event anime.

Starting in 1971, Giblett began researching bone marrow transplants with E. Donnall Thomas. Bone marrow transplantations were a pioneering technique used to treat blood cancers. At the time, if the donor and acceptor were the same sex, doctors could not confirm the success of the graft. Giblett assisted in discovering genetic markers that could confirm graft success, regardless of donor sex, using polymorphic blood proteins.

A dehydrogenase (also called DH or DHase in the literature) is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. They also catalyze the reverse reaction, for instance alcohol dehydrogenase not only oxidizes ethanol to acetaldehyde in animals but also produces ethanol from acetaldehyde in yeast.

If an intrinsic semiconductor is doped with a donor impurity then the majority carriers are electrons. If the semiconductor is doped with an acceptor impurity then the majority carriers are holes. Minority carriers play an important role in bipolar transistors and solar cells. Their role in field- effect transistors (FETs) is a bit more complex: for example, a MOSFET has p-type and n-type regions.

The tRNA(Tyr) molecule has an L-shaped structure. Its recognition involves both subunits of the tyrosyl-tRNA synthetase dimer. The acceptor arm of tRNA(Tyr) interacts with the catalytic domain of one YARS monomer whereas the anticodon arm interacts with the C-terminal moiety of the other monomer. In most YARS structures, the monomers are related to each other by a twofold rotational symmetry.

Rathayibacter toxicus is a chemoorganotroph that utilizes oxygen as its terminal electron acceptor. Using tubes of Medium C containing a variety of carbon sources, each 0.5% weight per volume concentration, noting growth and acid production for 4 weeks, it was determined that R. toxicus utilizes galactose, mannose, and xylose as carbon sources forming acidic byproducts. The production of acids from carbohydrates occurs oxidatively and weakly.

The organic semiconducting technology is replacing silicon and may one day achieve the goal of having a lab on a chip. The contorted aromatic molecules offer a wide variety of tuning and suitability options. Both electron acceptor (n-type) and electron donor (p-type) contorted molecules can be manufactured. The non-planer structure offers self-assembly characteristics leading to simultaneously optimized miscibility and phase separation.

An oxidase is an enzyme that catalyzes an oxidation-reduction reaction, especially one involving dioxygen (O2) as the electron acceptor. In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H2O) or hydrogen peroxide (H2O2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. The oxidases are a subclass of the oxidoreductases.

Na's beneficial effects include increases in p-type conductivity, texture, and average grain size. Furthermore, Na incorporation allows for performance to be maintained over larger stoichiometric deviations. Simulations have predicted that Na on an In site creates a shallow acceptor level and that Na serves to remove In on Cu defects (donors), but reasons for these benefits are controversial. Na is also credited with catalyzing oxygen absorption.

This means that real charge distribution and required solvent polarization are not in an "equilibrium". Yet it is possible that the solvent takes a configuration corresponding to the "transition state", even if the electron sits on the donor or acceptor. This, however, requires energy. This energy may be provided by the thermal energy of the solvent and thermal fluctuations can produce the correct polarization state.

The following diagrams represent several cases/situations of the application of the Basic Paxos protocol. Some cases show how the Basic Paxos protocol copes with the failure of certain (redundant) components of the distributed system. Note that the values returned in the Promise message are "null" the first time a proposal is made (since no Acceptor has accepted a value before in this round).

This results in the formation of formyl-H4MPT. :HCO-MF + H4MPT -> HCO-H4MPT + MF Formyl-H4MPT is subsequently reduced to methenyl-H4MPT. Methenyl-H4MPT then undergoes a one- step hydrolysis followed by a two-step reduction to methyl-H4MPT. The two-step reversible reduction is assisted by coenzyme F420 whose hydride acceptor spontaneously oxidizes. Once oxidized, F420’s electron supply is replenished by accepting electrons from H2.

Bacteriorhodopsin is a light-driven proton pump. It is the retinal molecule that changes its conformation when absorbing a photon, resulting in a conformational change of the surrounding protein and the proton pumping action. It is covalently linked to Lys216 in the chromophore by Schiff base action. After photoisomerization of the retinal molecule, Asp85 becomes a proton acceptor of the donor proton from the retinal molecule.

This process can be repeated as many times as necessary to achieve an efficient synthesis of a desired oligosaccharide with minimal loss of material to undesired coupling. This can be especially useful in “one-pot” synthetic methods. In these methods, multiple sugars are added to the reaction mixture. One of the sugars is armed as the glycosyl donor, and reacts quickly with a glycosyl acceptor.

Using two acceptor fluorophores rather than one, FRET can observe multiple sites for correlated movements and spatial changes in any complex molecule. This is shown in the research on the Holliday Junction. SmFRET with the three-color system offers insights on synchronized movements of junction's three helical sites and near non-existence of its parallel states. Ensemble FRET can use three-color system as well.

An exoelectrogen normally refers to a microorganism that has the ability to transfer electrons extracellularly. While exoelectrogen is the predominant name, other terms have been used: electrochemically active bacteria, anode respiring bacteria, and electricigens. Electrons exocytosed in this fashion are produced following ATP production using an electron transport chain (ETC) during oxidative phosphorylation. Conventional cellular respiration requires a final electron acceptor to receive these electrons.

Also in contrast to most other DIRB, G. fermentans cannot utilize elemental sulfur as an electron acceptor, a characteristic it shares with DIRB of the genera Geobacter. Geothrix fermentans can also employ fermentation, as its name implies, to oxidize substrates for energy production. This organism exhibited an ability to grow fermentatively on organic acids such as fumarate and citrate yielding acetate and succinate as fermentation products.

In a p-channel "depletion- mode" device, a positive voltage from gate to body widens the depletion layer by forcing electrons to the gate-insulator/semiconductor interface, leaving exposed a carrier-free region of immobile, positively charged acceptor ions. Conversely, in a p-channel "enhancement-mode" device, a conductive region does not exist and negative voltage must be used to generate a conduction channel.

They can use hydrogen as their electron donor and nitrate or sulphur as the electron acceptor. D. atlanticum can grow at temperatures between 50 °C and 80 °C, while optimal temperatures range between 70° and 75 °C. These bacteria can grow at pH ranges between 5 and 7.5, however preferred growth is at a pH of 6-6.2. D. atlanticum prefers low NaCl concentrations for optimal growth.

The lone pair repels more strongly than bond pairs, therefore the bond angle is not 109.5°, as expected for a regular tetrahedral arrangement, but 106.7°. This shape gives the molecule a dipole moment and makes it polar. The molecule's polarity, and especially, its ability to form hydrogen bonds, makes ammonia highly miscible with water. The lone pair makes ammonia a base, a proton acceptor.

When a tRNA with a complete[?] CCA sequence at its acceptor stem is bound to the A site, C74 of the tRNA stacking with U2590 (2555) induces a conformational change in the ribosome, resulting in movement of U2541 (2506), U2620 (2585) through G2618 (2583). The displacement of bases allows the ester group to adopt a new conformation accessible to nucleophilic attack from the A site.

The cyclic reaction is similar to that of the non-cyclic, but differs in that it generates only ATP, and no reduced NADP (NADPH) is created. The cyclic reaction takes place only at photosystem I. Once the electron is displaced from the photosystem, the electron is passed down the electron acceptor molecules and returns to photosystem I, from where it was emitted, hence the name cyclic reaction.

C60 has high electron affinity, making it a good acceptor. A C60/MEH-PPV double layer cell had a relatively high fill factor of 0.48 and a power conversion efficiency of 0.04% under monochromatic illumination. PPV/C60 cells displayed a monochromatic external quantum efficiency of 9%, a power conversion efficiency of 1% and a fill factor of 0.48. Perylene derivatives display high electron affinity and chemical stability.

Serine 92 is hydrogen bonded to His 201 in a fashion similar to various serine hyrdolases. however, instead of the carboxylic acid typically found in catalytic triads, the main chain carbonyl of Gln 250 serves as a hydrogen bond acceptor in an interaction with His 201. Two other residues, Arg-117 and Glu-11 are also located in the active site, but their function is not clear.

An electron acceptor is a chemical entity that accepts electrons transferred to it from another compound. It is an oxidizing agent that, by virtue of its accepting electrons, is itself reduced in the process. Electron acceptors are sometimes mistakenly called electron receptors. Typical oxidizing agents undergo permanent chemical alteration through covalent or ionic reaction chemistry, resulting in the complete and irreversible transfer of one or more electrons.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is D-aldohexoside:acceptor 3-oxidoreductase. Other names in common use include D-glucoside 3-dehydrogenase, D-aldohexopyranoside dehydrogenase, D-aldohexoside:cytochrome c oxidoreductase, D-glucoside 3-dehydrogenase, hexopyranoside-cytochrome c oxidoreductase, and D-aldohexoside:(acceptor) 3-oxidoreductase.

1,3-BPG has a very similar role in the Calvin cycle to its role in the glycolytic pathway. For this reason both reactions are said to be analogous. However the reaction pathway is effectively reversed. The only other major difference between the two reactions is that NADPH is used as an electron donor in the calvin cycle whilst NAD+ is used as an electron acceptor in glycolysis.

The first two substrates are released, but this ubisemiquinone intermediate remains bound. In the second step, a second molecule of QH2 is bound and again passes its first electron to a cytochrome c acceptor. The second electron is passed to the bound ubisemiquinone, reducing it to QH2 as it gains two protons from the mitochondrial matrix. This QH2 is then released from the enzyme.

Neohexene is prepared by ethenolysis of diisobutene, an example of a metathesis reaction: :(CH3)3C-CH=C(CH3)2 \+ CH2=CH2 → (CH3)3C-CH=CH2 \+ (CH3)2C=CH2 It is a building block to synthetic musks by its reaction with p-cymene. It is also used in the industrial preparation of terbinafine. In the study of C-H activation, neohexene is often used as a hydrogen acceptor.

DMSO reductase is a molybdenum-containing enzyme that catalyzes reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). This enzyme serves as the terminal reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then reduced to water. The reaction catalyzed by DMSO reductase.

Dissimilatory nitrate reduction to ammonium (DNRA), or nitrate/nitrite ammonification, is an anaerobic respiration process. Microbes which undertake DNRA oxidise organic matter and use nitrate as an electron acceptor, reducing it to nitrite, then ammonium (NO3−→NO2−→NH4+). Both denitrifying and nitrate ammonification bacteria will be competing for nitrate in the environment, although DNRA acts to conserve bioavailable nitrogen as soluble ammonium rather than producing dinitrogen gas.

On the contrary, there are lithotrophs that have the ability to ferment, implying their ability to convert organic carbon into another usable form. Lithotrophs play an important role in the biological aspect of the iron cycle. These organisms can use iron as either an electron donor, Fe(II) --> Fe(III), or as an electron acceptor, Fe (III) --> Fe(II). Another example is the cycling of nitrogen.

Assays evaluating lipid mixing make use of concentration dependent effects such as nonradiative energy transfer, fluorescence quenching and pyrene eximer formation. (1.) Illustration of lipid mixing assay based on Förster resonance energy transfer. (3.) Illustration of lipid mixing assay based on Fluorescence self-quenching. #NBD-Rhodamine Energy Transfer: In this method, membrane labeled with both NBD (donor) and Rhodamine (acceptor) combine with unlabeled membrane.

Passage of electrons between donor and acceptor releases energy, which is used to generate a proton gradient across the mitochondrial membrane by "pumping" protons into the intermembrane space, producing a thermodynamic state that has the potential to do work. This entire process is called oxidative phosphorylation since ADP is phosphrylated to ATP by using the electrochemical gradient established by the redox reactions of the electron transport chain.

For example, E. coli (a facultative anaerobe) does not have a cytochrome oxidase or a bc1 complex. Under aerobic conditions, it uses two different terminal quinol oxidases (both proton pumps) to reduce oxygen to water. Bacterial Complex IV can be split into classes according to the molecules act as terminal electron acceptors. Class I oxidases are cytochrome oxidases and use oxygen as the terminal electron acceptor.

Band structure of a p-type semiconductor. Dark circles in the conduction band are electrons and light circles in the valence band are holes. The image shows that the holes are the majority charge carrier P-type semiconductors are created by doping an intrinsic semiconductor with an electron acceptor element during manufacture. The term p-type refers to the positive charge of a hole.

3-dehydrosphinganine reductase catalyzes the chemical reaction: :sphinganine + NADP+ \rightleftharpoons 3-dehydrosphinganine + NADPH + H+ Thus, the two substrates of this enzyme are sphinganine and NADP+, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is ribitol:NAD+ 2-oxidoreductase. Other names in common use include adonitol dehydrogenase, ribitol dehydrogenase A (wild type), ribitol dehydrogenase B (mutant enzyme with different properties), and ribitol dehydrogenase D (mutant enzyme with different properties).

The protein encoded by this gene is a member of the glucuronyltransferase gene family. These enzymes exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product functions as the key enzyme in a glucuronyl transfer reaction during the biosynthesis of the carbohydrate epitope HNK-1 (human natural killer-1, also known as CD57 and LEU7). Alternate transcriptional splice variants have been characterized.

Most modern semiconductors are made by successive selective counterdoping steps to create the necessary P and N type areas.Hastings, Alan (2005) The Art of Analog Layout, 2nd ed. Although compensation can be used to increase or decrease the number of donors or acceptors, the electron and hole mobility is always decreased by compensation because mobility is affected by the sum of the donor and acceptor ions.

DsbD catalyses an essentially irreversible reaction due to the fact that electrons flow down their electrochemical gradient from inside the cell (negative inside) to outside the cell (positive outside). In order to reverse the reaction, electrons are transferred from dithiol proteins in the periplasm to an electron acceptor in the cytoplasm as follows: reduced proteinperiplasm → DsbAperiplasm → DsbBmembrane → quinonesmembrane → reductasemembrane→ terminal electron acceptorcytoplasm (e.g., O2, NO or fumarate).

Hydrogen atom diffusion on nanostructured graphitic carbon materials is primarily governed by physisorption of hydrogen atoms. Singled- walled nanotubes and multi-walled nanotubes are the best acceptor of spilt over hydrogen atoms. Another recent study has shown that the synthesis of methanol from both CO and CO2 over Cu/ZrO2 involves the spillover of H atoms formed on Cu to the surface of ZrO2.Jung, K-D.

On the other hand, intermolecular asymmetric reactions are quite confined to specifically matched combinations of acyl anion precursor and Michael acceptor, such as an aliphatic aldehyde with a nitroalkene.Jousseaume, T.; Wurz, N. E.; Glorius, F. Angew. Chem. Int. Ed. 2011, 50, 1410. In addition, these substrates tend to be rather activated, as the intermolecular asymmetric Stetter reaction is still in the early stages of development.

There is some concern that there is a physical limit to the available indium for ITO.Indium, USGS report Growth typically is performed in a reducing environment to compensating acceptor defects within the film (e.g. metal vacancies), which degrade the carrier concentration (if n-type). For AZO thin film deposition, the coating method of reactive magnetron sputtering is very economical and practical way of mass production.

Helicobacter typhlonius is a microaerophile capable of oxidative phosphorylation using oxygen as a terminal electron acceptor. In this species, fermentation of pyruvate and Acetyl-CoA to acetate is possible in the absence of oxygen. Additionally, carbohydrate breakdown includes both sucrose and mannose and amino acid degradation includes citrulline, aspartate, glutamate, and glutamine. H. typhlonius is also capable of arginine biosynthesis through the urea cycle.

The relative acceptor strength of Lewis acids toward a series of bases, versus other Lewis acids, can be illustrated by C-B plots.Laurence, C. and Gal, J-F. Lewis Basicity and Affinity Scales, Data and Measurement, (Wiley 2010) pp 50-51 IBSN 978-0-470-74957-9 The plots shown in this paper used older parameters. Improved E&C; parameters are listed in ECW model.

Monomers capable of forming single, double, triple or quadruple hydrogen bonding has been utilized for making supramolecular polymers, and increased association of monomers obviously possible when monomers have maximum number of hydrogen bonding donor/acceptor motifs. For instance, ureidopyrimidinone-based monomer with self-complementary quadruple hydrogen bonding termini polymerized in solution, accordingly with the theory of conventional polymers and displayed a distinct viscoelastic nature at ambient temperatures.

Takeharo Haino demonstrated an extreme example of sequence control in supramolecular copolymer, where three heteroditopic monomers are arranged in an ABC sequence along the copolymer chain. The design strategy utilizing three distinct binding interactions; ball-and-socket (calix[5]arene/C60), donor-acceptor (bisporphyrin/trinitrofluorenone), and Hamilton’s H-bonding interactions is the key to attain a high orthogonality to form an ABC supramolecular terpolymer.

In enzymology, a methanol dehydrogenase is an enzyme that catalyzes the chemical reaction: :methanol \rightleftharpoons formaldehyde + 2 electrons + 2H+ How the electrons are captured and transported depends upon the kind of methanol dehydrogenase and there are two main types. A common electron acceptor in biological systems is nicotinamide adenine dinucleotide (NAD+) and some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate (NADP+). An NAD+-dependent methanol dehydrogenase() was first reported in a Gram-positive methylotroph and is an enzyme that catalyzes the chemical reaction :methanol + NAD+ \rightleftharpoons formaldehyde + NADH + H+ Thus, the two substrates of this enzyme are methanol and NAD+, whereas its 3 products are formaldehyde, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is methanol:NAD+ oxidoreductase.

The characteristic feature of this absorption is a series of sharp lines called GR1-8, where GR1 line at 741 nm is the most prominent and important. The vacancy behaves as a deep electron donor/acceptor, whose electronic properties depend on the charge state. The energy level for the +/0 states is at 0.6 eV and for the 0/- states is at 2.5 eV above the valence band.

Depending on the structural and chemical environment, halogen bonding interactions can be weak or strong. In the case of some protein-ligand complexes, halogen bonds are energetically and geometrically comparable to that of hydrogen bonding if the donor-acceptor directionality remains consistent. This intermolecular interaction has been shown to be stabilizing and a conformational determinant in protein-ligand and DNA structures. For molecular recognition and binding, halogen bonding can be significant.

A more economically attractive option for treatment of the organic halides is through utilization of biological agents. Recently, bacteria (Ancylobacter aquaticus), fungi (Phanerochaete chrysosporium and Coiriolus versicolor), or synthetic enzymes have been used in the degradation of chlorinated organic compounds. The microorganisms degrade halocompounds using either aerobic or anaerobic processes. The mechanisms of degradation include utilization of the compound as carbon source for energy, cometabolite, or as an electron acceptor.

Guanine has the C-6 carbonyl group that acts as the hydrogen bond acceptor, while a group at N-1 and the amino group at C-2 act as the hydrogen bond donors. Guanine can be hydrolyzed with strong acid to glycine, ammonia, carbon dioxide, and carbon monoxide. First, guanine gets deaminated to become xanthine. Guanine oxidizes more readily than adenine, the other purine-derivative base in DNA.

This ratio can be used as a proxy of photoinhibition because more energy is emitted as fluorescence from Chlorophyll a when many excited electrons from PSII are not captured by the acceptor and decay back to their ground state. When measuring FV/FM, the leaf must be incubated in the dark for at least 10 minutes, preferably longer, before the measurement, in order to let non-photochemical quenching relax.

He is the god of fire and the acceptor of sacrifices. The sacrifices made to Agni go to the deities because Agni is a messenger from and to the other gods. He is ever-young, because the fire is re-lit every day, yet he is also immortal. In Indian tradition Fire is also linked to Surya or the Sun and Mangala or Mars, and with the south-east direction.

Arsenate can serve as a respiratory electron acceptor for oxidation of organic substrates and H2S or H2. Arsenates occur naturally in minerals such as adamite, alarsite, legrandite, and erythrite, and as hydrated or anhydrous arsenates. Arsenates are similar to phosphates since arsenic (As) and phosphorus (P) occur in group 15 (or VA) of the periodic table. Unlike phosphates, arsenates are not readily lost from minerals due to weathering.

In water, thiopyrylium reacts to it and forms a mixture of 2-hydroxythiopyran and 4-hydroxythiopyran. Thiopyrylium salts can be synthesized by hydrogen abstraction from thiopyran by a hydride ion acceptor, such as trityl perchlorate. The thiopyrylium analogue of 2,4,6-trisubstituted pyrylium salts can be synthesized by treatment with sodium sulfide followed by precipitation with acid. This reaction causes the oxygen atom in the pyrylium cation to be substituted with sulfur.

In chemistry, a cathode is the electrode of an electrochemical cell at which reduction occurs; a useful mnemonic to remember this is AnOx RedCat (Oxidation at the Anode = Reduction at the Cathode). Another mnemonic is to note the cathode has a 'c', as does 'reduction'. Hence, reduction at the cathode. Perhaps most useful would be to remember cathode corresponds to cation (acceptor) and anode corresponds to anion (donor).

Ladderane lipids present in anammoxosomes Ladderanes were first identified in a rare group of anaerobic ammonium oxidizing (anammox) bacteria belonging to the phylum Planctomycetes. These bacteria sequester the catabolic anammox reactions to intracellular compartments called anammoxosomes. The anammox process involves the oxidation of ammonium to nitrogen gas with nitrite as the final electron acceptor. Intermediates in this process are two highly toxic compounds, hydrazine (N2H4) and hydroxylamine (NH2OH).

3-O-alpha-D-glucosyl-L-rhamnose phosphorylase (, cphy1019 (gene)) is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose:phosphate beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction : 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose + phosphate \rightleftharpoons L-rhamnopyranose + beta-D-glucose 1-phosphate In the reverse phosphorolysis reaction the enzyme is specific for L-rhamnose as acceptor and beta-D-glucose 1-phosphate as donor.

Transamination catalyzed by aminotransferase occurs in two stages. In the first step, the α amino group of an amino acid is transferred to the enzyme, producing the corresponding α-keto acid and the aminated enzyme. During the second stage, the amino group is transferred to the keto acid acceptor, forming the amino acid product while regenerating the enzyme. The chirality of an amino acid is determined during transamination.

It is used in the Van Leusen reaction which is used to convert aldehydes to nitriles or in the preparation of oxazoles and imidazoles. The versatility of TosMIC in organic synthesis has been documented. It is a fairly strong carbon acid, with an estimated pKa of 14 (compared to 29 for methyl tolyl sulfone), the isocyano group acting as an electron acceptor of strength comparable to an ester group.

Introns are supposed to be removed, while the exons are expressed. The mutation must occur at the specific site at which intron splicing occurs: within non-coding sites in a gene, directly next to the location of the exon. The mutation can be an insertion, deletion, frameshift, etc. The splicing process itself is controlled by the given sequences, known as splice-donor and splice-acceptor sequences, which surround each exon.

Mutations in these sequences may lead to retention of large segments of intronic DNA by the mRNA, or to entire exons being spliced out of the mRNA. These changes could result in production of a nonfunctional protein. An intron is separated from its exon by means of the splice site. Acceptor-site and donor-site relating to the splice sites signal to the spliceosome where the actual cut should be made.

The extinction coefficient of the dye is 5700. It is soluble in dimethylformamide (DMF) or buffer above pH 6 and reacts primarily with thiols. The absorption spectrum IAEDANS overlaps well with the emission spectrum of tryptophan, making it useful as an acceptor in FRET experiments. It can also be used as a resonance energy donor to fluorophores such as fluorescein, Alexa Fluor 488, Oregon Green, and BODIPY FL.

Once the vesicles pinch off from the ER they are transported passively (by diffusion) or actively (by intracellular motors that run on cytoskeletal tracks). The mode of transport seems to be influenced by distance. Short distances may tend towards passive transport, whereas longer distances tend towards active transport. Once these vesicles reach their destination, they need to be first physically linked with their acceptor compartment (else they may float away).

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates () and related proteins into distinct sequence based families has been described. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

In combination with an alkenic acceptor, cyclization to either fused or bridged products takes place. Fused products are generally favored, unless the diazene precursor is substituted with electron-donating groups at the methylene carbon atom. The configuration of the alkene is maintained as long as the reaction is proceeding through a singlet TMM.Berson, J. A.; Duncan, C. D.; Corwin, L. R. J. Am. Chem. Soc. 1974, 96, 6175.

Hybrid solar cells combine advantages of both organic and inorganic semiconductors. Hybrid photovoltaics have organic materials that consist of conjugated polymers that absorb light as the donor and transport holes. Inorganic materials in hybrid cells are used as the acceptor and electron transporter in the structure. The hybrid photovoltaic devices have a potential for not only low-cost by roll-to-roll processing but also for scalable solar power conversion.

An energy diagram of the interface is shown in figure 1. In commonly used photovoltaic polymers such as MEH-PPV, the exciton binding energy ranges from 0.3 eV to 1.4 eV. The energy required to separate the exciton is provided by the energy offset between the LUMOs or conduction bands of the donor and acceptor. After dissociation, the carriers are transported to the respective electrodes through a percolation network.

Any reaction that decreases the overall Gibbs free energy of a system will proceed spontaneously (given that the system is isobaric and also adiabatic), although the reaction may proceed slowly if it is kinetically inhibited. The transfer of electrons from a high-energy molecule (the donor) to a lower-energy molecule (the acceptor) can be spatially separated into a series of intermediate redox reactions. This is an electron transport chain.

These FRET efficiencies can then be used to infer distances between molecules as a function against time. As the protein transitions between the folded and unfolded states, the corresponding distances between molecules can indicate the sequence of molecular interactions that lead to protein folding. Another application of smFRET is for DNA and RNA folding dynamics. Typically, two different locations of a nucleotide are labeled with the donor and acceptor dyes.

NEM is a Michael Acceptor in Michael Reaction, which means that it adds nucleophiles such as thiols. The resulting thioether features a strong C-S bond and the reaction is virtually irreversible. Reaction with thiols occur in the pH range 6.5–7.5, NEM may react with amines or undergo hydrolysis at a more alkaline pH. NEM has been widely used to probe the functional role of thiol groups in enzymology.

The process of halorespiration, or dehalorespiration, uses reductive dehalogenation to produce energy that can be used by the respiring microorganism to carry out its growth and metabolism. Halogenated organic compounds are used as the terminal electron acceptor, which results in their dehalogenation. Reductive dehalogenation is the process by which this occurs. It involves the reduction of halogenated compounds by removing the halogen substituents, while simultaneously adding electrons to the compound.

The iron cycle interacts significantly with the sulfur, nitrogen, and phosphorus cycles. Soluble Fe(II) can act as the electron donor, reducing oxidized organic and inorganic electron receptors, including O2 and NO3, and become oxidized to Fe(III). The oxidized form of iron can then be the electron acceptor for reduced sulfur, H2, and organic carbon compounds. This returns the iron to the oxidized Fe(II) state, completing the cycle.

In coordination chemistry, a pi-donor ligand is a kind of ligand endowed with filled non- bonding orbitals that overlap with metal-based orbitals. Their interaction is complementary to the behavior of pi-acceptor ligands. The existence of terminal oxo ligands for the early transition metals is one consequence of this kind of bonding. Classic pi-donor ligands are oxide (O2−), nitride (N3−), imide (RN2−), alkoxide (RO−), amide (R2N−), and fluoride.

However, as of 2013, researchers have been able to fabricate PSCs with fill factors of over 75%. Scientists have been able to accomplish via an inverted BHJ and by using nonconventional donor / acceptor combinations. However, efforts are being made to upscale manufacturing of polymer solar cells, in order to decrease costs and also advocate for a practical approach for PSC production. Such efforts include full roll-to-roll solution processing.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl- CoA:NADP+ cis-2-oxidoreductase. Other names in common use include NADPH- dependent cis-enoyl-CoA reductase, reductase, cis-2-enoyl coenzyme A, cis-2-enoyl-coenzyme A reductase, and cis-2-enoyl-CoA reductase (NADPH).

A three-layer (two acceptor and one donor) fullerene-free stack achieved a conversion efficiency of 8.4%. The implementation produced high open-circuit voltages and absorption in the visible spectra and high short-circuit currents. Quantum efficiency was above 75% between 400 nm and 720 nm wavelengths, with an open-circuit voltage around 1 V.Imec achieves record 8.4% efficiency in fullerene-free organic solar cells. Rdmag.com. Retrieved on 2015-11-12.

Polymer/polymer blends are also used in dispersed heterojunction photovoltaic cells. A blend of CN-PPV and MEH-PPV with Al and ITO as the electrodes, yielded peak monochromatic power conversion efficiency of 1% and fill factor of 0.38. Dye sensitized photovoltaic cells can also be considered important examples of this type. Issues Fullerenes such as PC71BM are often the electron acceptor materials found in high performing bulk heterojunction solar cells.

However, these electron acceptor materials very weakly absorb visible light, decreasing the volume fraction occupied by the strongly absorbing electron donor material. Furthermore, fullerenes have poor electronic tunability, resulting in restrictions placed on the development of conjugated systems with more appealing electronic structures for higher voltages. Recent research has been done on trying to replace these fullerenes with organic molecules that can be electronically tuned and contribute to light absorption.

After read through sORF A, the 80S scanning ribosome disassembles at the stop codon, which is the shunt take-off site. The 40S ribosomal subunits keep combining with RNA, and bypass the strong stem-loop structural element, land at the shunt acceptor site, resume scanning and reinitiate at the first long ORF. 5’-proximal sORF A and the stem-loop structure itself are two essential elements for CaMV shunting [5].

The net Eh between a given electron donor and acceptor; hydrogen ions and other species in place will determine which reaction will first take place. For instance, nitrification is hierarchically more favoured than sulphate reduction. This allows for enhanced oil recovery by disfavouring biologically produced H2S, which derives from reduced SO4. In this process, the effects of nitrate reduction on wettability, interfacial tension, viscosity, permeability, biomass and biopolymer production remain unknown.

In redox reactions involving metal ions, lone electrons can be transferred from the electron donor to the electron acceptor. That is, no other atoms or protons are transferred along with the electron in the redox reaction. For instance, consider the following reaction between iron and copper ions: Redox reaction with iron and copper ion. Iron ion serves as the reducing equivalent since it donates an electron to the copper ion.

This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle ( fixation). Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate (TPP) but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron- sulflur clusters.

Jablonski diagram of FRET with typical timescales indicated. Note that the black dashed line indicates a virtual photon. Förster resonance energy transfer (FRET), fluorescence resonance energy transfer (FRET), resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores). A donor chromophore, initially in its electronic excited state, may transfer energy to an acceptor chromophore through nonradiative dipole–dipole coupling.

In enzymology, a xylitol oxidase () is an enzyme that catalyzes the chemical reaction :xylitol + O2 \rightleftharpoons xylose + H2O2 Thus, the two substrates of this enzyme are xylitol and O2, whereas its two products are xylose and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is xylitol:oxygen oxidoreductase.

Some bacteria utilize thiosulfate anion as a terminal electron acceptor, reducing it to sulfide. If this occurs, the newly formed hydrogen sulfide () reacts with ferrous sulfate in the medium to form ferrous sulfide, which is visible as a black precipitate. Examples of sulfide-producing bacteria include Salmonella, Proteus, Citrobacter and Edwardsiella species. The blackening of the medium is almost always observed in the butt (bottom) of the medium.

Arsenate reductase (glutaredoxin) () is an enzyme that catalyzes the chemical reaction :arsenate + glutaredoxin \rightleftharpoons arsenite + glutaredoxin disulfide + H2O Thus, the two substrates of this enzyme are arsenate and glutaredoxin, whereas its 3 products are arsenite, glutaredoxin disulfide, and water. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is glutaredoxin:arsenate oxidoreductase.

Prezhdo pioneered time-dependent modeling of photo-induced electron transfer, relaxation and recombination in dye- sensitized semiconductors that form the basis for Gratzel solar cells,W. Stier and O. V. Prezhdo, “Non-adiabatic molecular dynamics simulation of light- induced electron transfer from an anchored molecular electron donor to a semiconductor acceptor”, J. Phys. Chem. B, 106 8047 (2002) providing a unified description for understanding molecule/bulk, organic/inorganic interfaces.

Cytochrome c Nitrite Reductase is a homodimer which contains five c-type heme cofactors per monomer. Four of the heme centers are bis- histidine ligated and presumably serve to shuttle electrons to the active site. The active site heme, however, is uniquely ligated by a single lysine residue. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with a cytochrome as acceptor.

In enzymology, a NAD(P)+ transhydrogenase (Re/Si-specific () is an enzyme that catalyzes the chemical reaction :NADPH + NAD+ \rightleftharpoons NADP+ \+ NADH Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. This enzyme participates in nicotinate and nicotinamide metabolism.

Human, murine and rat Pim-1 contain 313 amino acids, and have a 94 – 97% amino acid identity. The active site of the protein, ranging from amino acids 38-290, is composed of several conserved motifs, including a glycine loop motif, a phosphate binding site and a proton acceptor site. Modification of the protein at amino acid 67 (lysine to methionine) results in the inactivation of the kinase.

Cyclobis(paraquat-p-phenylene) is able to incorporate small guest molecules forming a host–guest complex. The interactions required for complex formation are donor-acceptor interactions and hydrogen bonding, their strength is highly dependent on the ability of the donor to provide π-electron density. Also an enlargement of the π-system enhances the binding. The kinetics of complex formation and dissociation depends on the bulkiness of the guest.

A typical Michael acceptor is an α,β-unsaturated ketone, although aldehydes and acid derivatives work as well. In addition, Bergmann et al. reports that donors such as nitriles, nitro compounds, sulfones and certain hydrocarbons can be used as acceptors. Overall, Michael acceptors are generally activated olefins such as those shown below where EWG refers to an electron withdrawing group such as cyano, keto, or ester as shown.

Thus, this allows for the decarboxylation of glutaconyl-CoA, an enzyme-bound intermediate, by breaking the Cγ-Cδ bond, resulting in formation of a dienolate anion, a proton, and CO2. The dienolate intermediate is protonated, resulting in crotonyl-CoA and a release of products from the active site. Finally, the 2e−-reduced form of FAD is oxidized to two 1e− steps by an external electron acceptor to complete the turnover.

He and his group showed that armed glycosyl donors could be coupled to a glycosyl acceptor, that was at the same time a disarmed glycosyl donor, without self-coupling of the disarmed donor/acceptor.D. R. Mootoo, P. Konradsson, U. Udodong, B. Fraser-Reid, J. Am. Chem. Soc. 1988, 110, 5583-5584. This approach allowed him to carry out a one-pot synthesis of a trisaccharide by the n-pentenyl glycoside method.

H. H. Jensen, L. Lyngbye, M. Bols, Angew. Chem. Int. Ed. 2001 40 3447-3449. Protection of a glycosyl donor with bulky silyl groups (tert- butyldimethylsilyl or triisopropyl) cause it to change conformation to a more axial-rich conformation that, as a consequence, is more reactive, which Bols and his group called superarmed. They showed that a superarmed donor can be coupled to an armed glycosyl donor/acceptor.

One of the downsides of using SMAs is the fact that, under atmospheric conditions, they tend to engage in disordered (anisotropic) states as a result of their planar structures. They are often planar as aromaticity is required for sufficient electron mobility. The lack of order may diminish electron transport and effective extraction routes that lead to induced current. Moreover, the corresponding lack of orientation affects donor-acceptor exciton formation.

The image demonstrates how ligase (yellow oval) catalyzes two DNA fragment strands. The ligase joins the two fragments of DNA to form a longer strand of DNA by "pasting" them together. The mechanism of DNA ligase is to form two covalent phosphodiester bonds between 3' hydroxyl ends of one nucleotide ("acceptor"), with the 5' phosphate end of another ("donor"). Two ATP molecules are consumed for each phosphodiester bond formed.

During the 1990s, the lactic acid hypothesis was created to explain why people experienced burning or muscle cramps that occurred during and after intense exercise. A lack of oxygen inside of the muscle cells resulted in lactic acid fermentation. This is due to the cell needing oxygen as a terminal electron acceptor to produce ATP. Without oxygen present, the cells needed to create energy through a different method.

Entries for the Melbourne Cup usually close during the first week of August. The initial entry fee is $600 per horse. Around 300 to 400 horses are nominated each year, but the final field is limited to 24 starters. Following the allocation of weights, the owner of each horse must on the four occasions before the race in November, declare the horse as an acceptor and pay a fee.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme is involved in the initial stages of the synthesis of bile acids from cholesterol and a member of the short-chain dehydrogenase/reductase superfamily. This enzyme is a membrane-associated endoplasmic reticulum protein which is active against 7-alpha hydrosylated sterol substrates.

Despite being a strained macrocycle, there exist an atropisomer, abyssomicin C. The atropisomerism arise due to a structural deviation in the α,β-unsaturated ketone region of the molecule. The orientation of the carbonyl in atrop- abyssomicin C is cisoid, whereas the conformation in abyssomicin C is transoid. The enone moiety of atrop-abyssomicin C has a higher degree of the conjugation, which makes it a more active Michael acceptor.

In enzymology, sarcosine dehydrogenase () is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is sarcosine:acceptor oxidoreductase (demethylating). Other names in common use include sarcosine N-demethylase, monomethylglycine dehydrogenase, and sarcosine:(acceptor) oxidoreductase (demethylating).

In enzymology, a phosphoenolpyruvate-glycerone phosphotransferase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + glycerone \rightleftharpoons pyruvate + glycerone phosphate Thus, the two substrates of this enzyme are phosphoenolpyruvate and glycerone, whereas its two products are pyruvate and glycerone phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is phosphoenolpyruvate:glycerone phosphotransferase.

The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus- containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase.

In enzymology, a testosterone 17beta-dehydrogenase is an enzyme that catalyzes the chemical reaction between testosterone and androst-4-ene-3,17-dione. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17beta-hydroxysteroid:NAD+ 17-oxidoreductase. Other names in common use include 17-ketoreductase and 17beta-HSD.

In enzymology, a hypotaurocyamine kinase () is an enzyme that catalyzes the chemical reaction :ATP + hypotaurocyamine \rightleftharpoons ADP + Nomega- phosphohypotaurocyamine Thus, the two substrates of this enzyme are ATP and hypotaurocyamine, whereas its two products are ADP and Nomega- phosphohypotaurocyamine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:hypotaurocyamine N-phosphotransferase.

The release of the electrons recycles the mediator to its original oxidized state, ready to repeat the process. This can happen only under anaerobic conditions; if oxygen is present, it will collect the electrons, as it has greater electronegativity. In MFC operation, the anode is the terminal electron acceptor recognized by bacteria in the anodic chamber. Therefore, the microbial activity is strongly dependent on the anode's redox potential.

B. Neritina biosynthetic pathway for bryostatins. In B. Neritina, bryostatin biosynthesis is carried out through a type I polyketide synthase cluster, bry. BryR is the secondary metabolism homolog of HMG-CoA synthase, which is the PKS in bacterial primary metabolism. In the bryostatin pathway, the BryR module catalyzes β-Branching between a local acetoacetyl acceptor acyl carrier protein (ACP-a) and an appropriate donor BryU acetyl-ACP (ACP-d).

Many compounds are derived from Fe(CO)5 by substitution of CO by Lewis bases, L, to give derivatives Fe(CO)5−xLx. Common Lewis bases include isocyanides, tertiary phosphines and arsines, and alkenes. Usually these ligands displace only one or two CO ligands, but certain acceptor ligands such as PF3 and isocyanides can proceed to tetra- and pentasubstitution. These reactions are often induced with a catalyst or light.

Due to the donor-acceptor-donor type structure, squaraine dyes such as Seta-670, Seta-700 and Seta-660 exhibit very high 2-photon absorption (2PA) efficiencies in comparison to other dyes, SeTau-647 and SeTau-665, a new type of squaraine- rotaxane, exhibit extremely high two-photon action cross-sections of up to 10,000 GM in the near IR region, unsurpassed by any other class of organic dyes.

The terminal helix (N) protrudes from the main body of the carboxy domain and this helix is reputed to play a role in mediating interactions with other subunits. Crystal structures demonstrate that this terminal N helix buries its hydrophobic surface into an acceptor pocket of an adjacent Cre subunit. The effect of the two-domain structure is to form a C-shaped clamp that grasps the DNA from opposite sides.

When base pairing with adenine, uracil acts as both a hydrogen bond acceptor and a hydrogen bond donor. In RNA, uracil binds with a ribose sugar to form the ribonucleoside uridine. When a phosphate attaches to uridine, uridine 5'-monophosphate is produced. Uracil undergoes amide-imidic acid tautomeric shifts because any nuclear instability the molecule may have from the lack of formal aromaticity is compensated by the cyclic-amidic stability.

In a 2004 research paper, ARL researchers explored how small concentrations of acceptor dopants can dramatically modify the properties of ferroelectric materials such as BST. Researchers "doped" BST thin films with magnesium, analyzing the "structure, microstructure, surface morphology and film/substrate compositional quality" of the result. The Mg doped BST films showed "improved dielectric properties, low leakage current, and good tunability", meriting potential for use in microwave tunable devices.

Ammonium is the only source of nitrogen. Annwoodia aquaesulis strains have been detected in mixed-population packed-bed reactors containing limestone as a source of carbon, elementary sulfur as the electron donor and nitrate as the terminal electron acceptor, as well as in karstic sulfidic thermal groundwater ecosystems of broad similarity to those from which the type strain was isolated Annwoodia aquaesulis grown on thiosulfate, tetrathionate or trithionate has high growth yields, which are broadly similar to those of Thermithiobacillus spp., and are higher than members of the closely related genus Thiobacillus, indicating core metabolic differences. This high yield was observed in spite of 70% more carbon dioxide being fixed than could be accounted for as biomass, indicating the excretion of a carbon intermediate, which is not observed in Thermithiobacillus tepidarius, which was isolated from the same location at the Roman Baths in Bath, also by enrichment culture on thiosulfate as the sole electron donor and molecular oxygen as the terminal electron acceptor.

Knallgas bacteria are a group of bacteria which are able to fix carbon dioxide using H2 as the electron donor and O2 as the terminal electron acceptor and energy source. Knallgas bacteria stand out from other hydrogen oxydizing bacteria which, although using H2 as an electron donor, are not able to fix CO2, as Knallgas do. This aerobic hydrogen oxidation, also known as the Knallgas reaction, which releases a considerable amount of energy, determines the generation of a proton motive force (PMF): H2 \+ O2 \longrightarrow H2O ΔGo = -237 kJ/mol The key enzymes involved in this reaction are the hydrogenases which lead the electrons through the electron transport chain, from hydrogen to the final acceptor, that is O2 which is actually reduced to water, the only product. The hydrogenases, which are divided into three categories according to the type of metal present in the active site, are the enzymes that allow the oxidation of hydrogen.

In general, "FRET" refers to situations where the donor and acceptor proteins (or "fluorophores") are of two different types. In many biological situations, however, researchers might need to examine the interactions between two, or more, proteins of the same type—or indeed the same protein with itself, for example if the protein folds or forms part of a polymer chain of proteins or for other questions of quantification in biological cells. Obviously, spectral differences will not be the tool used to detect and measure FRET, as both the acceptor and donor protein emit light with the same wavelengths. Yet researchers can detect differences in the polarisation between the light which excites the fluorophores and the light which is emitted, in a technique called FRET anisotropy imaging; the level of quantified anisotropy (difference in polarisation between the excitation and emission beams) then becomes an indicative guide to how many FRET events have happened.

The D1 (PsbA) and D2 (PsbD) photosystem II (PSII) reaction centre proteins from cyanobacteria, algae and plants only show approximately 15% sequence homology with the L and M subunits, however the conserved amino acids correspond to the binding sites of the photochemically active cofactors. As a result, the reaction centres (RCs) of purple photosynthetic bacteria and PSII display considerable structural similarity in terms of cofactor organisation. The D1 and D2 proteins occur as a heterodimer that form the reaction core of PSII, a multisubunit protein-pigment complex containing over forty different cofactors, which are anchored in the cell membrane in cyanobacteria, and in the thylakoid membrane in algae and plants. Upon absorption of light energy, the D1/D2 heterodimer undergoes charge separation, and the electrons are transferred from the primary donor (chlorophyll a) via phaeophytin to the primary acceptor quinone Qa, then to the secondary acceptor Qb, which like the bacterial system, culminates in the production of ATP.

Al Ghaffar gives the notion that Allah continuously and repetitively forgives an individual for his sins. If an individual returns to Allah and asks for repentance, it can be accepted due to Allah's Attribute of being Tawwab, the Acceptor of Repentance. Once Allah accepts the repentance of an individual through His Infinite Mercy, He can erase the sin altogether because of His Attribute, Affuw. It would be as though there is no sin at all.

The principal limitation of the solubility parameter approach is that it applies only to associated solutions ("like dissolves like" or, technically speaking, positive deviations from Raoult's law): it cannot account for negative deviations from Raoult's law that result from effects such as solvation or the formation of electron donor–acceptor complexes. Like any simple predictive theory, it can inspire overconfidence: it is best used for screening with data used to verify the predictions.

Halogen bond strengths range from 5–180 kJ/mol. The strength of XB allows it to compete with HB, which are a little bit weaker in strength. Halogen bonds tend to form at 180° angles, which was shown in Odd Hassel’s studies with bromine and 1,4-dioxane in 1954. Another contributing factor to halogen bond strength comes from the short distance between the halogen (Lewis acid, XB donor) and Lewis base (XB acceptor).

Under anaerobic conditions, the lack of oxygen requires that the bacteria use a different source for an electron acceptor. Common electron acceptors used by anaerobic bacteria are sulfate, iron, nitrate, manganese and carbon dioxide. The resulting products under anaerobic conditions are carbon dioxide (CO2), water (H2O), and methane (CH4). A simple chemical equation of the anaerobic process is: C6H12O6 → 3CO2 \+ 3CH Examples of anaerobic conditions for microbial biodegradation include soil and composts.

Al Ghaffar gives the notion that Allah continuously and repetitively forgives an individual for his sins. If an individual returns to Allah and asks for repentance, it can be accepted due to Allah's Attribute of being Tawwab, the Acceptor of Repentance. Once Allah accepts the repentance of an individual through His Infinite Mercy, He can erase the sin altogether because of His Attribute, Affuw. It would be as though there is no sin at all.

Reliability is an important consideration, and as a result, many specialized kiosk software applications have been developed for the industry. These applications interface with the bill acceptor and credit card swipe, meter time, prevent users from changing the configuration of software or downloading computer viruses and allow the kiosk owner to see revenue. Threats to reliability come from vulnerabilities to hacking, allowing access to the OS, and the need for a session or hardware restart.

The standard bacterial tmRNA consists of a tRNA(Ala)-like domain (allowing addition of a non-encoded alanine to mRNAs that happen to lack a stop coding), and an mRNA-like domain coding for a protein tag that destines the polypeptide for proteolysis. The mRNA-like domain was lost in mt-tmRNAs. Comparative sequence analysis indicates features typical for mt-tmRNAs. Most conserved is the primary sequence of the amino acyl acceptor stem.

The first n layer (the emitter) was formed because of the greater surface concentration of the donor (for example, antimony). The base formed beyond it because of the more rapid diffusion of the acceptor (for example, aluminum). The inner (collector) boundary of the base appeared where the diffused aluminum no longer over-compensated the n-type background doping of the original silicon. The base layers of the resulting transistors were 4 μm thick.

Cyanazine inhibits photosynthesis and is therefore used as a herbicide. It destroys unwanted vegetation, especially various types of weeds, grasses and woody plants. The primary site of inhibition was on the reducing side of photosystem II. They inhibit the electron transfer step between the primary electron acceptor (Q) and the plastoquinone pool of the electron transport chain. Cyanazine is the most toxic triazine herbicide and can cause birth defects, mutations and ultimately cancer.

JTB has been found to fuse with the telomeric repeats of acceptor telomeres in a case of JT. Homo sapiens JTB (hJTB) encodes a transmembrane protein that is highly conserved among divergent eukaryotic species. JT results in a hJTB truncation, which potentially produces an hJTB product devoid of the transmembrane domain. hJTB is located in a gene-rich region at 1q21, called epidermal differentiation complex (EDC). JTB has also been implicated in prostatic carcinomas.

The mechanism(s) of photoinhibition are under debate, several mechanisms have been suggested. Reactive oxygen species, especially singlet oxygen, have a role in the acceptor-side, singlet oxygen and low-light mechanisms. In the manganese mechanism and the donor side mechanism, reactive oxygen species do not play a direct role. Photoinhibited PSII produces singlet oxygen, and reactive oxygen species inhibit the repair cycle of PSII by inhibiting protein synthesis in the chloroplast.

Moreover, genome sequences provided unprecedented insights into the evolution of reductive dehalogenation and differing strategies for niche adaptation. Recently, it has become apparent that some organisms, including Desulfitobacterium chlororespirans, originally evaluated for halorespiration on chlorophenols, can also use certain brominated compounds, such as the herbicide bromoxynil and its major metabolite as electron acceptors for growth. Iodinated compounds may be dehalogenated as well, though the process may not satisfy the need for an electron acceptor.

Flavin Adenine Dinucleotide FAD, or flavin adenine dinucleotide, is a prosthetic group (a non-polypeptide unit bound to a protein that is required for function) that consists of an adenine nucleotide and a flavin mononucleotide. FAD is a unique electron acceptor. Its fully reduced form is FADH2 (known as the hydroquinone form), but FAD can also be partially oxidized as FADH by either reducing FAD or oxidizing FADH2. Dehydrogenases typically fully reduce FAD to FADH2.

The production of FADH is rare. The double-bonded nitrogen atoms in FAD make it a good acceptor in taking two hydrogen atoms from a substrate. Because it takes two atoms rather than one, FAD is often involved when a double bond is formed in the newly oxidized substrate. FAD is unique because it is reduced by two electrons and two protons, as opposed to both NAD+ and NADP, which only take one proton.

Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. A single- nucleotide polymorphism (C825T) in this gene is associated with essential hypertension and obesity. This polymorphism is also associated with the occurrence of the splice variant GNB3-s, which appears to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites.

The contorted PAHs owing to their non-polar and non-planar topology and shape are expected to offer a balance between miscibility and self- aggregation for optimal charge transport to electrodes. These contorted conjugated aromatic molecules support the charge transport due to resonance of electrons and hinder the possibility of electron hole pair recombination for having suitable HOMO and LUMO offsets at donor and acceptor interphase while allowing the antagonistic charge percolation pathways.

On his turn, DsbB is reoxidized by transferring electrons to oxidized ubiquinone, which passes them to cytochrome oxidases, which finally reduce oxygen; this is in aerobic conditions. As molecular oxygen serves as the terminal electron acceptor in aerobic conditions, oxidative folding is conveniently coupled to it through the respiratory chain. In anaerobic conditions however, DsbB passes its electrons to menaquinone, followed by a transfer of electrons to fumarate reductase or nitrate reductase.

The defective gene associated with LCCS1 is mRNA export mediator GLE1 at chromosome 9q34. In more than 40 families the fetus has been homozygous for A->G substitution (c.432-10A>G) located in intron 3 of GLE1 creating an illegitimate splice acceptor site resulting in nine extra nucleotides in the GLE1 cDNA (GLE1 FinMajor mutation). In one family the fetus has been compound heterozygous for GLE1 FinMajor and R→H substitution in exon 12.

400px Photoinduced electron transfer (PET) is an excited state electron transfer process by which an excited electron is transferred from donor to acceptor."Highlights of the spectroscopy, photochemistry and electrochemistry of [M(CO)4(α-diimine)] complexes, M=Cr, Mo, W" Antonín Vlcek Coord. Chem. Rev. 230 (2002) 225-242."Organic and Inorganic Photochemistry" V. Ramamurthy and Kirk S. Schanze 1998 Marcel Dekker Due to PET a charge separation is generated, i.e.

This can happen when another Proposer, unaware of the new value being decided, starts a new round with a higher identification number n. In that case, the Acceptor can promise and later accept the new proposed value even though it has accepted another one earlier. These proposals may even have different values in the presence of certain failures. However, the Paxos protocol will guarantee that the Acceptors will ultimately agree on a single value.

In most deployments of Paxos, each participating process acts in three roles; Proposer, Acceptor and Learner. This reduces the message complexity significantly, without sacrificing correctness: By merging roles, the protocol "collapses" into an efficient client-master-replica style deployment, typical of the database community. The benefit of the Paxos protocols (including implementations with merged roles) is the guarantee of its safety properties. A typical implementation's message flow is covered in the section Multi-Paxos.

The pharmacophore model of PDE5 usually consists of one hydrogen bond acceptor, one hydrophobic aliphatic carbon chain and two aromatic rings. Small hydrophobic pocket and H-loop of PDE5 enzyme are important for binding affinity of PDE5 inhibitors. As well as positional and conformational changes are observed upon inhibitor binding in many cases. The active site of PDE5 is located at a helical bundle domain at the center of C domain (catalytic domain).

These enzymes catalyse sialyltransfer reactions during glycosylation, and are type II membrane proteins. There are about twenty different sialyltransferases which can be distinguished on the basis of the acceptor structure on which they act and on the type of sugar linkage they form. For example, a group of sialyltransferases adds sialic acid with an alpha-2,3 linkage to galactose, while other sialyltransferases add sialic acid with an alpha-2,6 linkage to galactose or N-acetylgalactosamine.

Treatment of (OC)5M=B-Tp with carbon monoxide or acetonitrile yields the corresponding adducts: (CO)2B-Tp and (MeNC)2B-Tp. Bis(CAAC)BH HOMO. Bonding in these complexes is quite similar to that in mono- Lewis base compounds. At least one π-acceptor ligand is present in all known examples of these compounds, and the B-L bond strength tends to scale with the π-acidity of the Lewis base.

She studied the photoluminescence decay dynamics of QDs and phosphors in the time and frequency domains. Several interesting discoveries came from this work. In CdS QDs, the surface ligands strongly affect the functional form of the decay; with trap states giving rise to broadband emission and a stretched exponential decay with long characteristic lifetimes. The nonexponential decay dynamics of the complex donor-acceptor phosphor ZnS:Cu,Al are a strong function of the excitation conditions.

Cumpstey, I. Carbohydr. Res. 2008, 343, 1553–1573 In this approach, the glycosyl acceptor is tethered onto the C-2-O-protecting group (X) in the first step. Upon activation of the glycosyl donor group (Y) (usually SR, OAc, or Br group) in the next step, the tethered aglycon traps the developing oxocarbenium ion at C-1, and is transferred from the same face as OH-2, forming the glycosidic bond stereospecifically.

At MIT, they discovered a pattern in the genetic code regarding the residue hydropathy and molar volume of encoded amino acids. Youvan has also published research in the fields of digital imaging spectroscopy for absorption spectra and fluorescence, including Fluorescence Resonance Energy Transfer (FRET). Zeiss has incorporated "Youvan's Method" into their Axiomat microscope for algorithmic deconvolution of the actual FRET signal in an image (such as GFP interactions) from interfering donor and acceptor spectral signals.

Cryptand with a metal cation demonstrating host–guest chemistry. Cryptands are tricyclic compounds that tightly encapsulate the guest cation via electrostatic interactions (ion-dipole interaction). Chemists use the study of intramolecular and intermolecular non- covalent bonding/interactions in molecules to evaluate reactivity. Such interactions include, but are not limited to, hydrogen bonding, electrostatic interactions between charged molecules, dipole-dipole interactions, polar-π and cation-π interactions, π-stacking, donor-acceptor chemistry, and halogen bonding.

T. litoralis grows near shallow and deep sea hydrothermal vents in extremely hot water. The optimal growth temperature for T. litoralis is 85–88 °C. It also prefers slightly acidic waters, growing between pH 4.0 to 8.0 with the optimal pH between 6.0-6.4. Unlike many other hyperthermophiles, T. litoralis is only facultatively dependent on sulfur as a final electron acceptor in fermentation, producing hydrogen gas in its absence and hydrogen sulfide when present.

PCBM is the common abbreviation for the fullerene derivative [6,6]-phenyl-C61-butyric acid methyl ester. It is being investigated in organic solar cells. PCBM is a fullerene derivative of the C60 buckyball that was first synthesized in the 1990s. It is an electron acceptor material and is often used in organic solar cells (plastic solar cells) or flexible electronics in conjunction with electron donor materials such as P3HT or other conductive polymers.

The researchers proposed a semi-transparent PSC with enhanced efficiency that utilizes both narrow bandgap polymer donor, PTB7‐Th, and non-fullerene acceptor, IHIC. The results of this study showed that the proposed PSC exhibited high transmittance and absorption in the infrared spectrum but low absorption in the visible spectrum. This cell showed to be relatively stable and have a maximum PCE of 9.77%, which, as of 2017, is the highest reported PCE value.

In enzymology, a zeatin reductase () is an enzyme that catalyzes the chemical reaction :dihydrozeatin + NADP+ \rightleftharpoons zeatin + NADPH + H+ Thus, the two substrates of this enzyme are dihydrozeatin and NADP+, whereas its 3 products are zeatin, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrozeatin:NADP+ oxidoreductase.

Polymer Solar Cells fabricated from chloronaphthalene (CN) as a co-solvent enjoy a higher efficiency than those fabricated from the more conventional pure chlorobenzene solution. This is because the donor- acceptor morphology changes, which reduces the phase separation between donor polymer and fullerene. As a result, this translates into high hole mobilities. Without co-solvents, large domains of fullerene form, decreasing photovoltaic performance of the cell due to polymer aggregation in solution.

Nicotinamide adenine dinucleotide (NAD+), a derivative of vitamin B3 (niacin), is an important coenzyme that acts as a hydrogen acceptor. Hundreds of separate types of dehydrogenases remove electrons from their substrates and reduce NAD+ into NADH. This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to reduce their substrates. Nicotinamide adenine dinucleotide exists in two related forms in the cell, NADH and NADPH.

One approach involves using a sliding window, which traverses the sequence data in an overlapping manner. The output at each position is a score based on whether the network thinks the window contains a donor splice site or an acceptor splice site. Larger windows offer more accuracy but also require more computational power. A neural network is an example of a signal sensor as its goal is to identify a functional site in the genome.

Acetylindoxyl oxidase () is an enzyme that catalyzes the chemical reaction :N-acetylindoxyl + O2 \rightleftharpoons N-acetylisatin + (?) Thus, the two substrates of this enzyme are N-acetylindoxyl and oxygen, whereas its product is N-acetylisatin. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is N-acetylindoxyl:oxygen oxidoreductase. This enzyme participates in tryptophan metabolism.

In particular, D576 acts as a proton acceptor to activate the nucleophilic hydroxyl oxygen on substrate serine or threonine residues, allowing the phosphate transfer reaction to occur mediated by base-catalysis. DFG Motif D594, F595, and G596 compose a motif central to B-Raf's function in both its inactive and active state. In the inactive state, F595 occupies the nucleotide-binding pocket, prohibiting ATP from entering and decreasing the likelihood of enzyme catalysis.

In 2019 his research group isolated a uranium(V)-dinitrogen complex.Lu, Erli; Atkinson, Benjamin, E.; Wooles, Ashley J.; Boronski, Josef T.; Doyle, Laurence R.; Tuna, Floriana; Cryer, Jonathan D.; Cobb, Philip J.; Vitorica-Yrezabal, Inigo J.; Whitehead, George F. S.; Kaltsoyannis, Nikolas; Liddle, Stephen T. (2019) “Back-bonding between an electron-poor, high-oxidation-state metal and poor π-acceptor ligand in a uranium(V)–dinitrogen complex”. Nature Chemistry. 11, 806-811.

MVK can act as an alkylating agent because it is an effective Michael acceptor. It gained early attention for its use in the Robinson annulation, a method useful in the preparation of steroids: Robinson annulation reaction Its alkylating ability is both the source of its high toxicity and the feature that makes it a useful intermediate in organic synthesis. MVK will polymerize spontaneously. The compound is typically stored with hydroquinone, which inhibits polymerization.

Perylene diimide derivatives are a good candidate as acceptor materials due to their high electron affinity and high electron mobilities. Highly stable organic solar cells with high electron mobility have been reported in scientific literature.Usta, H., Facchetti, A., Marks, T. J. (2011) n-Channel Semiconductor Materials Design for Organic Complementary Circuits. Acc. Chem. Res. 44, 501−510 The HOMO/LUMO levels of perylene diimide derivatives can easily be tuned via substitution at the bay position.

The type species of the genus is D. lykanthroporepellens ( Moe et al. 2009). The species epithet derives from the Greek noun lykanthropos (λυκάνθρωπος), werewolf; Latin participle adjective repellens, repelling; New Latin participle adjective lykanthroporepellens, repelling `werewolves, because compounds exhibiting a pungent garlic aroma are produced when these organisms grow in the presence of 1,2,3-trichloropropane as an electron acceptor and sulfide as a reducing agent, garlic being said to repel werewolves in some fiction literature.

Some species have the ability of chemolitho-autotrophic growth by means of sulfide oxidation for energy and with carbon dioxide as a source of carbon for biosynthesis. In this metabolism internal stored nitrate is the electron acceptor and reduced to ammonia. ::Sulfide oxidation: 2H2S + O2 → 2S + 2H2O Marine autotrophic Beggiatoa species are able to oxidize intracellular sulfur to sulfate. A frequently occurring mechanism when oxygen is lacking is reduction of elemental sulfur.

In the late 1970s, it was shown that there is a single stranded covalently closed, i.e. circular form of RNA expressed throughout the animal and plant kingdom (see circRNA). circRNAs are thought to arise via a "back-splice" reaction where the spliceosome joins a downstream donor to an upstream acceptor splice site. So far the function of circRNAs is largely unknown, although for few examples a microRNA sponging activity has been demonstrated.

In eukaryotes, NADH is the most important electron donor. The associated electron transport chain is NADH → Complex I → Q → Complex III → cytochrome c → Complex IV → O2 where Complexes I, III and IV are proton pumps, while Q and cytochrome c are mobile electron carriers. The electron acceptor is molecular oxygen. In prokaryotes (bacteria and archaea) the situation is more complicated, because there are several different electron donors and several different electron acceptors.

A ketone enolate is an enolate formed from a ketone by reaction with a strong base, such as lithium diisopropylamide, or with a Lewis acid such as dibutylboron trifluoromethanesulfonate and a weak base such as N,N-diisopropylethylamine. In the latter case, the base takes the hydrogen ion from the alpha carbon of the ketone and the electron acceptor atom of the Lewis acid becomes attached to the oxygen of the ketone.

In enzymology, a cyclopentanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :cyclopentanol + NAD+ \rightleftharpoons cyclopentanone + NADH + H+ Thus, the two substrates of this enzyme are cyclopentanol and NAD+, whereas its 3 products are cyclopentanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclopentanol:NAD+ oxidoreductase.

In enzymology, a hexadecanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :hexadecanol + NAD+ \rightleftharpoons hexadecanal + NADH + H+ Thus, the two substrates of this enzyme are hexadecanol and NAD+, whereas its 3 products are hexadecanal, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanol:NAD+ oxidoreductase.

In enzymology, a hydroxymalonate dehydrogenase () is an enzyme that catalyzes the chemical reaction :hydroxymalonate + NAD+ \rightleftharpoons oxomalonate + NADH + H+ Thus, the two substrates of this enzyme are hydroxymalonate and NAD+, whereas its 3 products are oxomalonate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydroxymalonate:NAD+ oxidoreductase.

In enzymology, a geraniol dehydrogenase () is an enzyme that catalyzes the chemical reaction :geraniol + NADP+ \rightleftharpoons geranial + NADPH + H+ Thus, the two substrates of this enzyme are geraniol and NADP+, whereas its 3 products are geranial, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geraniol:NADP+ oxidoreductase.

In enzymology, a xylitol kinase () is an enzyme that catalyzes the chemical reaction :ATP + xylitol \rightleftharpoons ADP + xylitol 5-phosphate Thus, the two substrates of this enzyme are ATP and xylitol, whereas its two products are ADP and xylitol 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:xylitol 5-phosphotransferase.

In enzymology, a sulcatone reductase () is an enzyme that catalyzes the chemical reaction :sulcatol + NAD+ \rightleftharpoons sulcatone + NADH + H+ Thus, the two substrates of this enzyme are sulcatol and NAD+, whereas its 3 products are sulcatone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is sulcatol:NAD+ oxidoreductase.

In enzymology, a guanylate kinase () is an enzyme that catalyzes the chemical reaction :ATP + GMP \rightleftharpoons ADP + GDP Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP.

In enzymology, a (−)-borneol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(−)-borneol + NAD \rightleftharpoons (−)-camphor + NADH + H Thus, the two substrates of this enzyme are (−)-borneol and NAD, whereas its 3 products are (−)-camphor, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-borneol:NAD oxidoreductase.

While aerobic organisms during respiration use oxygen as a terminal electron acceptor, anaerobic organisms use other electron acceptors. These inorganic compounds have a lower reduction potential than oxygen, meaning that respiration is less efficient in these organisms and leads to slower growth rates than aerobes. Many facultative anaerobes can use either oxygen or alternative terminal electron acceptors for respiration depending on the environmental conditions. Most respiring anaerobes are heterotrophs, although some do live autotrophically.

Acetogenesis is a type of microbial metabolism that uses hydrogen () as an electron donor and carbon dioxide () as an electron acceptor to produce acetate, the same electron donors and acceptors used in methanogenesis (see above). Bacteria that can autotrophically synthesize acetate are called homoacetogens. Carbon dioxide reduction in all homoacetogens occurs by the acetyl-CoA pathway. This pathway is also used for carbon fixation by autotrophic sulfate-reducing bacteria and hydrogenotrophic methanogens.

125x125pxSilylones are a class of zero-valent monatomic silicon complexes, characterized as having two lone pairs and two donor-acceptor ligand interactions stabilizing a silicon(0) center. Synthesis of silylones generally involves the use of sterically bulky carbenes to stabilize highly reactive Si(0) centers. For this reason, silylones are sometimes referred to siladicarbenes. To date, silylones have been synthesized with cyclic alkyl amino carbenes (cAAC) and bidentate N-heterocyclic carbenes (bis-NHC).

General structure of trisilaallene. The structure of carbene-stabilized silylones were first predicted using theoretical calculations by Gernot Frenking and coworkers in 2009. Their theoretical study of silylones was inspired from the development and synthesis of carbones: an analogous structure containing carbon(0) stabilized by two donor-acceptor ligand interactions. It was also inspired by previous reports of trisilaallene: a silylene complex featuring a bent geometry about the Si-Si-Si center.

Beta-1,4-galactosyltransferase 4 is an enzyme that in humans is encoded by the B4GALT4 gene. This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures.

For example, iodoperfluoroalkanes are well-designed for XB crystal engineering. In addition, this is also why F2 can act as a strong XB donor, but fluorocarbons are weak XB donors because the alkyl group connected to the fluorine is not electronegative. In addition, the Lewis base (XB acceptor) tends to be electronegative as well and anions are better XB acceptors than neutral molecules. Halogen bonds are strong, specific, and directional interactions that give rise to well-defined structures.

Blood 1998; 92:1707-1712 Other possible defects in PS translocation, reported in some patients, require further study.Weiss, HJ: Impaired platelet procoagulant mechanisms in patients with bleeding disorders. Sem. Thromb. Hemost. 35:233-241, 2009 The initially reported patient with Scott Syndrome has been found to have a mutation at a splice-acceptor site of the gene encoding transmembrane protein 16F (TMEM16F).Suzuki J, Umeda M, Sims PJ, Nagata S. Calcium-dependent phospholipid scrambling by TMEM16F.

NAD(P)H dehydrogenase [quinone] 1 is an enzyme that in humans is encoded by the NQO1 gene. This protein-coding gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a 2-electron reductase (enzyme). This FAD-binding protein forms homodimers and performs two-electron reduction of quinones to hydroquinones and of other redox dyes. It has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone.

On the other hand, for semiconductors, the behavior of transistors and other devices can be very different depending on whether there are many electrons with low mobility or few electrons with high mobility. Therefore mobility is a very important parameter for semiconductor materials. Almost always, higher mobility leads to better device performance, with other things equal. Semiconductor mobility depends on the impurity concentrations (including donor and acceptor concentrations), defect concentration, temperature, and electron and hole concentrations.

Taicatoxin acts on the voltage-dependent L-type calcium channels from the heart, and on the small conductance Ca2+-activated K+ channels in the chromaffin cells and in the brain. It has a high affinity for the 125I-apamin acceptor-binding sites of the rat synaptosomal membranes (Ki = 1.45±0.22 nM) and blocks affinity-labeling of a 33-kDa 125I-apamin-binding polypeptide. Other neurotoxins that act on the calcium channels are calcicludine, calciseptine, ω-conotoxin, ω-agatoxin.

O-Desilylation and oxidation of the resulting alcohol produce an acceptor for a Horner-Wadsworth-Emmons reaction, wherein a carbonyl and an alpha-methylated phosphonate react to produce an alkene. In this case, a beta-keto phosphonate bearing an (R)-phenylglycine- derived auxiliary group was ligated to the molecule. This group is lost in asymmetric conjugate addition of an (R)-amino alcohol, which, through two cyclodehydration steps using Wipf's oxazoline-thiazoline interconversion protocol, produces the thiazoline ring.

However, inhibition of PSII membranes under anaerobic conditions leads primarily to inhibition of electron transfer on the acceptor side of PSII. Ultraviolet light causes inhibition of the oxygen-evolving complex before the rest of PSII becomes inhibited. Photosystem I (PSI) is less susceptible to light-induced damage than PSII, but slow inhibition of this photosystem has been observed. Photoinhibition of PSI occurs in chilling-sensitive plants and the reaction depends on electron flow from PSII to PSI.

Beta-1,4-galactosyltransferase 3 is an enzyme that in humans is encoded by the B4GALT3 gene. This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures.

The metals in ionic bonding usually lose their valence electrons, becoming a positively charged cation. The nonmetal will gain the electrons from the metal, making the nonmetal a negatively charged anion. As outlined, ionic bonds occur between an electron donor, usually a metal, and an electron acceptor, which tends to be a nonmetal. Hydrogen bonding occurs when a hydrogen atom bonded to an electronegative atom forms an electrostatic connection with another electronegative atom through interacting dipoles or charges.

The final reduction of the fumarate is achieved in the active site where the asymmetrical charges from the nearby amino acids polarize the fumarate and distort its shape. Once the fumarate is no longer planar, a hydride from the bound FAD molecule in the active site attacks the double bond to reduce the fumarate. Thus, in this reaction, the fumarate serves as the terminal electron acceptor. Pathway for electron tunneling across the fumarate reductase with distances labeled in Angstroms.

One paper-based biosensor that can be used to detect Salmonella, as well as E. coli, uses the nanomaterial graphene. These strips are a form of lateral flow assay, where the test line is composed of fluorescence antibody- labeled CdSe/ZnS quantum dots (Ab-QDs) as probes. After the sample has been applied, graphene oxide is added and it functions as the revealing agent. An energy transfer takes place between a donor molecule and an acceptor molecule.

Proton transfer and elimination of the cyanide ion affords benzoin as the product. This is a reversible reaction, which means that the distribution of products is determined by the relative thermodynamic stability of the products and starting material. Mechanism of the benzoin addition In this reaction, one aldehyde donates a proton and one aldehyde accepts a proton. Some aldehydes can only donate protons, such as 4-dimethylaminobenzaldehyde whereas benzaldehyde is both a proton acceptor and donor.

Time-resolved fluorescence energy transfer (TR-FRET) is the practical combination of time-resolved fluorometry (TRF) with Förster resonance energy transfer (FRET) that offers a powerful tool for drug discovery researchers. TR-FRET combines the low background aspect of TRF with the homogeneous assay format of FRET. The resulting assay provides an increase in flexibility, reliability and sensitivity in addition to higher throughput and fewer false positive/false negative results. FRET involves two fluorophores, a donor and an acceptor.

The biological fluids or serum commonly used in these research applications contain many compounds and proteins which are naturally fluorescent. Therefore, the use of conventional, steady-state fluorescence measurement presents serious limitations in assay sensitivity. Long-lived fluorophores, such as lanthanides, combined with time-resolved detection (a delay between excitation and emission detection) minimizes prompt fluorescence interference. This method (commonly referred to as time-resolved fluorometry or TRF) involves two fluorophores: a donor and an acceptor.

The biosynthesis of disaccharides, oligosaccharides, and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2, and Gls3 from yeast. 1,3-Beta-glucan synthase () also known as callose synthase catalyses the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall.

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene. The protein encoded by this gene is a member of the glucuronyltransferase gene family, enzymes that exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product catalyzes the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans.

In comparison to N-demthylases, another class of caffeine-degrading enzymes, caffeine dehydrogenase does not require the use of oxygen, NAD, or NADP as electron acceptors. Instead, caffeine dehydrogenase uses dichlorophenol, indophenol, coenzyme Q0, and cytochrome c as electron acceptors. Caffeine dehydrogenase has been noted as being more stable as well. Caffeine dehydrogenase is responsible for catalyzing the oxidation of caffeine directly into trimethyluric acid, and the enzyme uses coenzyme Q0, also known as ubiquinone, as an electron acceptor.

This oxidation relies on a combination of chemically and microbiologically catalyzed processes. Two electron acceptors can influence this process: O2 and Fe3+ ions. The latter will only be present in significant amounts in acidic conditions (pH < 2.5). First a slow chemical process with O2 as electron acceptor will initiate the oxidation of pyrite: :FeS2 \+ 7/2 O2 \+ H2O → Fe2+ \+ 2 SO42− \+ 2 H+ This reaction acidifies the environment and the Fe2+ will be formed is rather stable.

Between these spheres a certain amount of charge is reversibly exchanged. In the first step the energy WI of the transfer of a specific amount of charge is calculated, e.g. for the system in a state when both spheres carry half of the amount of charge which is to be transferred. This state of the system can be reached by transferring the respective charge from the donor sphere to the vacuum and then back to the acceptor sphere.

Paxos describes the actions of the processors by their roles in the protocol: client, acceptor, proposer, learner, and leader. In typical implementations, a single processor may play one or more roles at the same time. This does not affect the correctness of the protocol—it is usual to coalesce roles to improve the latency and/or number of messages in the protocol. ; Client: The Client issues a request to the distributed system, and waits for a response.

Beta-1,4-galactosyltransferase 2 is an enzyme that in humans is encoded by the B4GALT2 gene. This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures.

Hydrogen oxidizing bacteria are a group of facultative autotrophs that can use hydrogen as an electron donor. They can be divided into aerobes and anaerobes. The former use hydrogen as an electron donor and oxygen as an acceptor while the latter use sulphate or nitrogen dioxide as electron acceptors. Some species of both bacteria types have been isolated in different environments, for example in fresh waters, sediments, soils, activated sludge, hot springs, hydrothermal vents and percolating water.

Beta-1,4-galactosyltransferase 5 is an enzyme that in humans is encoded by the B4GALT5 gene. This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures.

They are usually processed from solution employing variable deposition techniques including simple spin-coating, ink-jet deposition or industrial reel-to-reel coating which allows preparing thin films on a flexible substrate. The materials of choice are conjugated polymers such as poly- thiophene, poly-phenylenevinylene, and copolymers of alternating donor and acceptor units such as members of the poly(carbazole-dithiophene- benzothiadiazole (PCDTBT) family. For solar cell applications they can be blended with C60 or PCBM as electron acceptors.

Hydrocyanation is, most fundamentally, the process whereby H+ and -CN ions are added to a molecular substrate. Usually the substrate is an alkene and the product is a nitrile. When -CN is a ligand in a transition metal complex, its basicity makes it difficult to dislodge, so, in this respect, hydrocyanation is remarkable. Since cyanide is both a good σ-donor and π-acceptor its presence accelerates the rate of substitution of ligands trans from itself, the trans effect.

CPOX is an enzyme involved in the sixth step of porphyrin metabolism it catalyses the oxidative decarboxylation of coproporphyrinogen III to proto-porphyrinogen IX in the haem and chlorophyll biosynthetic pathways. The protein is a homodimer containing two internally bound iron atoms per molecule of native protein. The enzyme is active in the presence of molecular oxygen that acts as an electron acceptor. The enzyme is widely distributed having been found in a variety of eukaryotic and prokaryotic sources.

Normally planar, this distortion exposes the lone pair of electrons on the nitrogen in ring A to the Fe+2 ion. Subsequent investigation revealed a 100o distortion in protoporphyrin bound to human ferrochelatase. A highly conserved histidine residue (His183 in B. subtilis, His263 in humans) is essential for determining the type of distortion, as well as acting as the initial proton acceptor from protoporphyrin. Anionic residues form a pathway facilitating proton movement away from the catalytic histidine.

There is a basic moiety connected to a carbon chain linked to an aromatic moiety by an amide bridge. The amide bridge can be inverted without affecting the potency of the agonist. A biaryl group shows more potency than a monoaryl group as the aromatic moiety and substitution at position 2 on the later aryl group will further increase the potency. Potency is higher for agonists with H+ donor/acceptor on the later aryl group on the biaryl group.

Copper (II) bromide in chloroform-ethyl acetate reacts with ketones resulting in the formation of alpha-bromo ketones. The resulting product can be directly used for the preparation of derivatives. This heterogeneous method is reported to be the most selective and direct method of formation of α-bromo ketones. Dibromination of NPGs, n-pentenyl glycosides, using CuBr2/LiBr reagent combination was performed in order for an NPG to serve as a glycosyl acceptor during halonium-promoted couplings.

Arginase's active site is extraordinarily specific. Modifying the substrate structure and/or stereochemistry severely lowers the kinetic activity of the enzyme. This specificity occurs due to the high number of hydrogen bonds between substrate and enzyme; direct or water-facilitated hydrogen bonds exist, saturating both the four acceptor positions on the alpha carboxylate group and all three positions on the alpha amino group. N-hydroxy-L-arginine (NOHA), an intermediate of NO biosynthesis, is a moderate inhibitor of arginase.

Two siblings and two unrelated individuals with Miller syndrome were studied. They looked at variants that have the potential to be pathogenic such as non-synonymous mutations, splice acceptor and donor sites and short coding insertions or deletions. Since Miller syndrome is a rare disorder, it is expected that the causal variant has not been previously identified. Previous exome sequencing studies of common single nucleotide polymorphisms (SNPs) in public SNP databases were used to further exclude candidate genes.

In this method, the glycosyl donor is protected at C-2 by a para-methoxybenzyl (PMB) group. The glycosyl acceptor is then tethered at the benzylic position of the PMB protecting group in the presence of 2,3-Dichloro-5,6-dicyano-1,4-benzoquinone (DDQ). The anomeric leaving group (Y) is then activated, and the developing oxocarbenium ion is captured by the tethered aglycon alcohol (OR) to give 1,2-cis β-glycoside product.Ito, Y.; Ogawa, T. Angew. Chem. Int.

Indol derivatives with 1-NH of 2-indolinone motif that is an H-bond donor, and 2-carbonyl oxygen that acts as an H-bond acceptor, bind with Glu915 and Cys917, respectively. These compounds have basic amine side chains or nitrogen heterocycles and provide ideal solubility and pharmacokinetics. These compounds are promising anti-cancer and anti-fibrosis agents, inhibiting various protein tyrosine kinases. They have higher efficiency, lower toxicity, fewer side effects, favorable preparation technology and favorable physicochemical properties.

In formal language theory his papers examined the relationships between grammar-based systems, acceptor-based systems, and algebraic characterizations of families of languages. The culmination of this work was the creation of one of the deepest branches of Computer Science, Abstract Families of Languages, in collaboration with Sheila Greibach in 1967. In 1974, Ginsburg, along with Armin B. Cremers, developed the theory of Grammar Forms. In the 1980s, Ginsburg became an early pioneer in the field of Database Theory.

If the photon collection efficiencies of the two channels are similar and the actual FRET distance is not interested, one can set the two \eta = 1, and the two quantum yields to 1 as well. (A) An example time trajectory of the acceptor (red) and donor (blue) channel photon counts collected at 1 ms time resolution. (B) Data binned into 10 ms time resolution to reduce the noise. The inset shows the smFRET time trajectory calculated with the equation.

Formation of supermicelles from various block copolymers: a hydroxyl- functionalized polymethylvinylsiloxane (HD), an H-bonding acceptor block poly(2-vinylpyridine) (HA), a non-interactive block poly(tert-butyl acrylate (N), and a crosslinkable block poly(methylvinylsiloxane) (X). Polyferrocenyldimethylsilane (PFS) is used as the supermicelle core. Bottom row shows electron microscopy images recorded after evaporation of the solvent, scale bars are 500 nm (100 nm in the insets). Electron micrograph of a windmill-like supermicelle, scale bar 500 nm.

Some anaerobic fermenting microbes in the rumen (and other gastrointestinal tracts) are capable of degrading organic matter to short chain fatty acids, and hydrogen. The accumulating hydrogen inhibits the microbe's ability to continue degrading organic matter, but syntrophic hydrogen-consuming microbes allow continued growth by metabolizing the waste products. In addition, fermentative bacteria gain maximum energy yield when protons are used as electron acceptor with concurrent H2 production. Hydrogen-consuming organisms include methanogens, sulfate-reducers, acetogens, and others.

Lewis acids have been classified in the ECW model and it has been shown that there is no one order of acid strengths. The relative acceptor strength of Lewis acids toward a series of bases, versus other Lewis acids, can be illustrated by C-B plots.Laurence, C. and Gal, J-F. Lewis Basicity and Affinity Scales, Data and Measurement, (Wiley 2010) pp 50-51 IBSN 978-0-470-74957-9 The plots shown in this paper used older parameters.

A third, only marginally related concept was proposed in 1923 by Gilbert N. Lewis, which includes reactions with acid-base characteristics that do not involve a proton transfer. A Lewis acid is a species that accepts a pair of electrons from another species; in other words, it is an electron pair acceptor. Brønsted acid-base reactions are proton transfer reactions while Lewis acid-base reactions are electron pair transfers. Many Lewis acids are not Brønsted-Lowry acids.

Oligosaccharides have diverse structures. The number of monosaccharides, ring size, the different anomeric stereochemistry, and the existence of the branched-chain sugars all contribute to the amazing complexity of the oligosaccharide structures. The essence of the reducing oligosaccharide synthesis is connecting the anomeric hydroxyl of the glycosyl donors to the alcoholic hydroxyl groups of the glycosyl acceptors. Protection of the hydroxyl groups of the acceptor with the target alcoholic hydroxyl group unprotected can assure the regiochemical control.

In enzymology, a xanthommatin reductase () is an enzyme that catalyzes the chemical reaction :5,12-dihydroxanthommatin + NAD+ \rightleftharpoons xanthommatin + NADH + H+ Thus, the two substrates of this enzyme are 5,12-dihydroxanthommatin and NAD+, whereas its 3 products are xanthommatin, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,12-dihydroxanthommatin:NAD+ oxidoreductase.

In enzymology, a dihydrouracil oxidase () is an enzyme that catalyzes the chemical reaction :5,6-dihydrouracil + O2 \rightleftharpoons uracil + H2O2 Thus, the two substrates of this enzyme are 5,6-dihydrouracil and O2, whereas its two products are uracil and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is 5,6-dihydrouracil:oxygen oxidoreductase. It employs one cofactor, FMN.

In enzymology, a beta-nitroacrylate reductase () is an enzyme that catalyzes the chemical reaction :3-nitropropanoate + NADP+ \rightleftharpoons 3-nitroacrylate + NADPH + H+ Thus, the two substrates of this enzyme are 3-nitropropanoate and NADP+, whereas its 3 products are 3-nitroacrylate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-nitropropanoate:NADP+ oxidoreductase.

The oxidation potential (Eh, measured in volts) is, as in any reaction system, the thermodynamic driving force of anaerobic respiration, which takes place in oxygen depleted environments. Prokaryotes are among the cells that have anaerobic respiration as metabolic strategy for survival. The electron transport takes place along and across the cellular membrane (prokaryotes lack of mitochondria). Electrons are transferred from an electron donor (molecule to be oxidised anaerobically) to an electron acceptor (NO3, SO4, MnO4, etc.).

TCNQ achieved great attention because it forms charge- transfer salts with high electrical conductivity. These discoveries were influential in the development of organic electronics. Illustrative is the product from treatment of TCNQ with the electron donor tetrathiafulvene (TTF), TCNQ forms an ion pair, the TTF-TCNQ complex, in which TCNQ is the acceptor. This salt crystallizes in a one-dimensionally stacked polymer, consisting of segregated stacks of cations and anions of the donors and the acceptors, respectively.

Kinases should not be confused with phosphorylases, which catalyze the addition of inorganic phosphate groups to an acceptor, nor with phosphatases, which remove phosphate groups (dephosphorylation). The phosphorylation state of a molecule, whether it be a protein, lipid or carbohydrate, can affect its activity, reactivity and its ability to bind other molecules. Therefore, kinases are critical in metabolism, cell signalling, protein regulation, cellular transport, secretory processes and many other cellular pathways, which makes them very important to human physiology.

For example, superimposed phenyl rings might be referred to more conceptually as an 'aromatic ring' pharmacophore element. Likewise, hydroxy groups could be designated as a 'hydrogen-bond donor/acceptor' pharmacophore element. # Validation – A pharmacophore model is a hypothesis accounting for the observed biological activities of a set of molecules that bind to a common biological target. The model is only valid insofar as it is able to account for differences in biological activity of a range of molecules.

Persistence length measurement of single stranded DNA is viable by various tools. Most of them have been done by incorporation of the worm-like chain model. For example, two ends of single stranded DNA were tagged by donor and acceptor dyes to measure average end to end distance which is represented as FRET efficiency. It was converted to persistence length by comparing the FRET efficiency with calculated FRET efficiency based on models such as the worm-like chain model.

In enzymology, a glutathione oxidase () is an enzyme that catalyzes the chemical reaction :2 glutathione + O2 \rightleftharpoons glutathione disulfide + H2O2 Thus, the two substrates of this enzyme are glutathione and O2, whereas its two products are glutathione disulfide and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione metabolism.

In enzymology, a cyclohexylamine oxidase () is an enzyme that catalyzes the chemical reaction :cyclohexylamine + O2 \+ H2O \rightleftharpoons cyclohexanone + NH3 \+ H2O2 The 3 substrates of this enzyme are cyclohexylamine, O2, and H2O, whereas its 3 products are cyclohexanone, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is cyclohexylamine:oxygen oxidoreductase (deaminating). This enzyme participates in caprolactam degradation.

In enzymology, a glyoxylate oxidase () is an enzyme that catalyzes the chemical reaction :glyoxylate + H2O + O2 \rightleftharpoons oxalate + H2O2 The 3 substrates of this enzyme are glyoxylate, H2O, and O2, whereas its two products are oxalate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is glyoxylate:oxygen oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a pyridoxal oxidase () is an enzyme that catalyzes the chemical reaction :pyridoxal + H2O + O2 \rightleftharpoons 4-pyridoxate + (?) The 3 substrates of this enzyme are pyridoxal, H2O, and O2, whereas its product is 4-pyridoxate. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 metabolism.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating). Other names in common use include triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, and glyceraldehyde-3-P-dehydrogenase.

In enzymology, a fluoroacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :fluoroacetaldehyde + NAD+ \+ H2O \rightleftharpoons fluoroacetate + NADH + 2 H+ The 3 substrates of this enzyme are fluoroacetaldehyde, NAD+, and H2O, whereas its 3 products are fluoroacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is fluoroacetaldehyde:NAD+ oxidoreductase.

As mentioned above, the ability to synthesize anti- diols from allylic alcohols can be achieved with the use of NMO as a stoichiometric oxidant. The use of tetramethylenediamine (TMEDA) as a ligand produced syn-diols with a favorable diastereomeric ratio compared to Kishi’s protocol; however, stoichiometric osmium is employed. Syn-selectivity is due to the hydrogen bond donor ability of the allylic alcohol and the acceptor ability of the diamine. This has since been applied to homoallylic systems.

A mixture of mercury and thallium vapour, when irradiated with the light of the mercury resonance line, shows the emission spectra of both atoms. Since thallium atoms do not absorb the exciting light, they can get excited only indirectly by an excitation transfer from mercury atoms. A transfer by reabsorption is impossible here. Therefore, this transfer must be a non- radiative one with a mercury atom as the donor or sensitizer and the thallium atom as the acceptor.

Irbesartan was developed by Sanofi Research and is longer acting than valsartan and losartan and it has an imidazolinone ring where a carbonyl group functions as a hydrogen bond acceptor instead of the hydroxymethyl group in losartan. Irbesartan is a non- competitive inhibitor. Candesartan cilexetil (TCV 116) is a benzimidazole which was developed at Takeda and is an ester carbonate prodrug. In vivo, it is rapidly converted to the much more potent corresponding 7-carboxylic acid, candesartan.

Beta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene. This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures.

This method allows you to recombine at least 9 different fragments in an acceptor vector by using type 2 restriction enzyme which cuts outside of the restriction sites. It begins with sub cloning of fragments in separate vectors to create Bsa1 flanking sequences on both sides. These vectors are then cleaved using type II restriction enzyme Bsa1, which generates four nucleotide single strand overhangs. Fragments with complementary overhangs are hybridized and ligated using T4 DNA ligase.

Other cofactors, such as ATP and coenzyme A, were discovered later in the 1900s. The mechanism of cofactor activity was discovered when, Otto Heinrich Warburg determined in 1936 that NAD+ functioned as an electron acceptor. Well after these initial discoveries, scientists began to realize that the manipulation of cofactor concentrations could be used as tools for the improvement of metabolic pathways. An important group of organic cofactors is the family of molecules referred to as vitamins.

NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (NDUFS4) also known as NADH-ubiquinone oxidoreductase 18 kDa subunit is an enzyme that in humans is encoded by the NDUFS4 gene. This gene encodes an nuclear-encoded accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I, or NADH:ubiquinone oxidoreductase). Complex I removes electrons from NADH and passes them to the electron acceptor ubiquinone. Mutations in this gene can cause mitochondrial complex I deficiencies such as Leigh syndrome.

The plot distinguishes between main chain-main chain, main chain-side chain and side chain-side chain hydrogen bonding interactions. Bifurcated hydrogen bonds and multiple hydrogen bonds between amino acid residues; and intra- and interchain hydrogen bonds are also indicated on the plots. Three classes of hydrogen bondings are distinguished by color-coding; short (distance smaller than 2.5 Å between donor and acceptor), intermediate (between 2.5 Å and 3.2 Å) and long hydrogen bonds (greater than 3.2 Å).

Halostagnicola larsenii is a halophilic, neutrophilic, chemo-organotroph and uses oxygen as its terminal electron acceptor. H. larsenii can utilize a variety of carbohydrates such as fructose, glycerol, lactose, glucose, arabinose, acetate, ribose, starch, maltose, galactose, ribose, xylose, glutamate, and propionate as substrates for growth. Growth substrates were determined through the use of the isolation medium, which contained the substrate being tested along with yeast extract. Additionally, H. larsenii undergoes assimilatory nitrate reduction to nitrite to ammonia.

In enzymology, an allyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction :allyl alcohol + NADP+ \rightleftharpoons acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and NADP+, whereas its 3 products are acrolein, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase.

In enzymology, a cyclohexanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :cyclohexanol + NAD+ \rightleftharpoons cyclohexanone + NADH + H+ Thus, the two substrates of this enzyme are cyclohexanol and NAD+, whereas its 3 products are cyclohexanone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cyclohexanol:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.

UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase removes a UMP and glucuronokinase, with the cofactor ADP, removes the final phosphate leading to -glucuronic acid. The aldehyde group of this compound is reduced to a primary alcohol using the enzyme glucuronate reductase and the cofactor NADPH, yielding -gulonic acid. This is followed by lactone formationutilizing the hydrolase gluconolactonasebetween the carbonyl on C1 and hydroxyl group on C4.

In enzymology, a T2-induced deoxynucleotide kinase () is an enzyme that catalyzes the chemical reaction :ATP + dGMP (or dTMP) \rightleftharpoons ADP + dGDP (or dTDP) The 3 substrates of this enzyme are ATP, dGMP, and dTMP, whereas its 3 products are ADP, dGDP, and dTDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)NMP phosphotransferase.

In enzymology, a thiamine-diphosphate kinase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction :thiamine diphosphate + ATP \rightleftharpoons thiamine triphosphate + ADP Thus, the two substrates of this enzyme are ATP and thiamine diphosphate, whereas its two products are ADP and thiamine triphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:thiamine-diphosphate phosphotransferase.

In enzymology, an acetate kinase (diphosphate) () is an enzyme that catalyzes the chemical reaction :diphosphate + acetate \rightleftharpoons phosphate + acetyl phosphate Thus, the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate-acetate phosphotransferase.

In enzymology, an opheline kinase () is an enzyme that catalyzes the chemical reaction :ATP + guanidinoethyl methyl phosphate \rightleftharpoons ADP + N'-phosphoguanidinoethyl methylphosphate Thus, the two substrates of this enzyme are ATP and guanidinoethyl methyl phosphate, whereas its two products are ADP and N'-phosphoguanidinoethyl methylphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus- containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoethyl-methyl- phosphate phosphotransferase.

In enzymology, a phosphoenolpyruvate-protein phosphotransferase () is an enzyme that catalyzes the chemical reaction :phosphoenolpyruvate + protein histidine \rightleftharpoons pyruvate + protein Npi-phospho-L-histidine Thus, the two substrates of this enzyme are phosphoenolpyruvate and protein histidine, whereas its two products are pyruvate and protein Npi-phospho-L- histidine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in phosphotransferase system (pts).

In enzymology, a macrolide 2'-kinase () is an enzyme that catalyzes the chemical reaction :ATP + oleandomycin \rightleftharpoons ADP + oleandomycin 2'-O-phosphate Thus, the two substrates of this enzyme are ATP and oleandomycin, whereas its two products are ADP and oleandomycin 2'-O-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:macrolide 2'-O-phosphotransferase.

In enzymology, a 3-hydroxyacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-3-hydroxyacyl-CoA + NAD+ \rightleftharpoons 3-oxoacyl-CoA + NADH + H+ Thus, the two substrates of this enzyme are (S)-3-hydroxyacyl-CoA and NAD+, whereas its 3 products are 3-oxoacyl-CoA, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.

In enzymology, a tetrahydroxynaphthalene reductase () is an enzyme that catalyzes the chemical reaction :scytalone + NADP+ \rightleftharpoons 1,3,6,8-tetrahydroxynaphthalene + NADPH + H+ Thus, the two substrates of this enzyme are scytalone and NADP+, whereas its 3 products are 1,3,6,8-tetrahydroxynaphthalene, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is scytalone:NADP+ Delta5-oxidoreductase.

In enzymology, a formate kinase () is an enzyme that catalyzes the chemical reaction :ATP + formate \rightleftharpoons ADP + formyl phosphate Thus, the two substrates of this enzyme are ATP and formate, whereas its two products are ADP and formyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:formate phosphotransferase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

In enzymology, a deoxyadenosine kinase () is an enzyme that catalyzes the chemical reaction :ATP + deoxyadenosine \rightleftharpoons ADP + dAMP Thus, the two substrates of this enzyme are ATP and deoxyadenosine, whereas its two products are ADP and dAMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyadenosine 5'-phosphotransferase. This enzyme is also called purine-deoxyribonucleoside kinase.

In enzymology, a (deoxy)adenylate kinase () is an enzyme that catalyzes the chemical reaction :ATP + dAMP \rightleftharpoons ADP + dADP Thus, the two substrates of this enzyme are ATP and dAMP, whereas its two products are ADP and dADP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)AMP phosphotransferase. This enzyme participates in purine metabolism.

In enzymology, a lombricine kinase () is an enzyme that catalyzes the chemical reaction :ATP + lombricine \rightleftharpoons ADP + N-phospholombricine The two substrates of this enzyme are ATP and lombricine, and the two products are ADP and N-phospholombricine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.

In enzymology, a glutamate 1-kinase () is an enzyme that catalyzes the chemical reaction :ATP + L-glutamate \rightleftharpoons ADP + alpha-L-glutamyl phosphate Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and alpha-L-glutamyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 1-phosphotransferase.

In enzymology, a guanidinoacetate kinase () is an enzyme that catalyzes the chemical reaction :ATP + guanidinoacetate \rightleftharpoons ADP + phosphoguanidinoacetate Thus, the two substrates of this enzyme are ATP and guanidinoacetate, whereas its two products are ADP and phosphoguanidinoacetate. Guanidinoacetate kinase belongs to the family of transferases, specifically those that transfer phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoacetate N-phosphotransferase. This enzyme is also called glycocyamine kinase.

A (−)-menthol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(−)-menthol + NADP \rightleftharpoons (−)-menthone + NADPH + H, i.e., catalyses the breakdown of menthol. Thus, the two substrates of this enzyme are (−)-menthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (−)-menthol:NADP oxidoreductase.

In enzymology, an omega-hydroxydecanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :10-hydroxydecanoate + NAD+ ⇌ 10-oxodecanoate + NADH + H+ Thus, the two substrates of this enzyme are 10-hydroxydecanoate and NAD+, whereas its 3 products are 10-oxodecanoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-hydroxydecanoate:NAD+ 10-oxidoreductase.

In enzymology, a butyrate kinase () is an enzyme that catalyzes the chemical reaction :ADP + butyryl-phosphate \rightleftharpoons ATP + butyrate Thus, the two substrates of this enzyme are ADP and butyryl-phosphate, whereas its two products are ATP and butyrate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:butanoate 1-phosphotransferase. This enzyme participates in butyrate metabolism.

During photosynthesis, natural electron acceptor NADP is reduced to NADPH in chloroplasts. The following equilibrium reaction takes place. A reduction reaction that stores energy as NADPH: :NADP+ + 2H+ + 2e- -> NADPH + H+ (Reduction) An oxidation reaction as NADPH's energy is used elsewhere: :NADP+ + 2H+ + 2e- <\- NADPH + H+ (Oxidation) Ferredoxin, also known as a NADH+ reductase, is an enzyme that catalyzes the reduction reaction. It is easy to oxidize NADPH but difficult to reduce NADP+, hence a catalyst is beneficial.

The addition of DCPIP experimentally to a chlorophyll molecule containing solution which shows a change in color due to the reduction of DCPIP It is possible to introduce an artificial electron acceptor into the light reaction, such as a dye that changes color when it is reduced. These are known as Hill reagents. These dyes permitted the finding of electron transport chains during photosynthesis. Dichlorophenolindophenol (DCPIP), an example of these dyes, is widely used by experimenters.

Field effect: Top panels: An applied voltage bends bands, depleting holes from surface (band diagram, left). The charge inducing the bending is balanced by a layer of negative acceptor-ion charge (right). Bottom panel: A larger applied voltage further depletes holes but conduction band lowers enough in energy to populate an inversion layer. In physics, the field effect refers to the modulation of the electrical conductivity of a material by the application of an external electric field.

A recent study of human circRNAs revealed that these molecules are usually composed of 1–5 exons. Each of these exons can be up to 3x longer than the average expressed exon, suggesting that exon length may play a role in deciding which exons to circularize. 85% of circularized exons overlap with exons that code for protein, although the circular RNAs themselves do not appear to be translated. During circRNA formation, exon 2 is often the upstream "acceptor" exon.

Further work extended the scope of this reaction to include aliphatic aldehydes as well.Moore, J. L.; Kerr, M. S.; Rovis, T. Tetrahedron 2006, 62, 11477. Subsequently, it was shown that the olefin geometry of the Michael acceptor dictates diastereoselectivity in these reactions, whereby the catalyst dictates the enantioselectivity of the initial carbon bond formation and allylic strain minimization dictates the diastereoselective intramolecular protonation.de Alaniz, J. R.; Rovis, T. J. Am. Chem. Soc. 2005, 127, 6284. Scheme 10.

Remember that a hole is created by an acceptor atom, e.g. Boron, which has one less electron than Silicon. One might ask how can holes be repelled if they are actually non-entities? The answer is that what really happens is not that a hole is repelled, but electrons are attracted by the positive field, and fill these holes, creating a depletion region where no charge carriers exist because the electron is now fixed onto the atom and immobile.

Members of the proposed genus Scalindua are anaerobic anammox (ammonium oxidizing) bacteria. The ammonium- oxidizing reaction composes a significant part of the global nitrogen cycle; by some estimates it is the cause of up to 50% of total nitrogen turnover in marine environments. It consists of the oxidization of ammonium using nitrite as an electron acceptor (both are fixed nitrogen) and subsequent generation of nitrogen gas: “NH4+ \+ NO2− = N2 \+ 2H2O (ΔG° = -357 kj mol-1)” This reaction uses nitrite (NO2−) as a terminal electron acceptor to produce nitric oxide (NO), which is then combined with ammonium (NH4+) to produce the intermediate hydrazine (N2H4) and water (H2O). Hydrazine, a very reactive molecule also used for rocket fuel, is then oxidized into nitrogen gas (N2). The half reactions may be represented as: “NO2− \+ 2H+ \+ e− = NO + H2O (E° = +0.38V) NO + NH4+ \+ 2H+ \+ 3e− = N2H4 \+ H2O (E° = +0.06V) Mechanism of Ammonium Oxidation N2H4 = N2 \+ 4H+ \+ 4e− (E° = -0.75V)” This metabolic pathway occurs anaerobically, something that was once considered impossible as ammonium was thought to be inert in the absence of oxygen.

A filtered-popping recursive transition network (FPRTN),Javier M. Sastre, "Efficient parsing using filtered-popping recursive transition networks", Lecture Notes in Artificial Intelligence, 5642:241-244, 2009 or simply filtered-popping network (FPN), is a recursive transition network (RTN) William A. Woods, "Transition network grammars for natural language analysis", Communications of the ACM, ACM Press, 13:10:591-606, 1970 extended with a map of states to keys where returning from a subroutine jump requires the acceptor and return states to be mapped to the same key. RTNs are finite-state machines that can be seen as finite-state automata extended with a stack of return states; as well as consuming transitions and \varepsilon-transitions, RTNs may define call transitions. These transitions perform a subroutine jump by pushing the transition's target state onto the stack and bringing the machine to the called state. Each time an acceptor state is reached, the return state at the top of the stack is popped out, provided that the stack is not empty, and the machine is brought to this state.

When combined with the free radical-forming TCNQ as an acceptor molecule, it can mimic the mechanism of metallic magnets. The magnetic properties arise from the fully pi-conjugated nitrogen-containing backbone combined with molecular charge transfer side groups. These properties cause the molecule to have a high density of localized spins that can give rise to coupling of their magnetic fields. When this polymer magnet is synthesized, the polymer chains need 3 months to line up before displaying any notable magnetism.

In enzymology, an aldehyde ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction :an aldehyde + H2O + 2 oxidized ferredoxin an acid + 2 H+ \+ 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a relatively rare example of a tungsten-containing protein.

Additionally, all of the sets of halogen bonding interactions are not identical, and all of the intermolecular interactions between halogen and halogen bond acceptor slightly exceed the sum of the Van der Waals radius, signifying a slightly weaker halogen bond, which leads to more flexibility in the structure. The 2D layers stack parallel to each other to produce channels filled with solvent. 2-D layers of 2:3CHCl3. Halogen bonds are shown in red, and the solvent molecules are not shown.

The biosyntheses of rosmarinic acid uses 4-coumaroyl-CoA from the general phenylpropanoid pathway as hydroxycinnamoyl donor. The hydroxycinnamoyl acceptor substrate comes from the shikimate pathway: shikimic acid, quinic acid and 3,4-dihydroxyphenyllactic acid derived from L-tyrosine. Thus, chemically, rosmarinic acid is an ester of caffeic acid with 3,4-dihydroxyphenyllactic acid, but biologically, it is formed from 4-coumaroyl-4'-hydroxyphenyllactate. Rosmarinate synthase is an enzyme that uses caffeoyl-CoA and 3,4-dihydroxyphenyllactic acid to produce CoA and rosmarinate.

In the second step, degalactosylation, the covalent bond is broken when Glu461 accepts a proton, replacing the galactose with water. Two transition states occur in the deep site of the enzyme during the reaction, once after each step. When water participates in the reaction, galactose is formed, otherwise, when D-glucose acts as the acceptor in the second step, transgalactosylation occurs . It has been kinetically measured that single tetramers of the protein catalyze reactions at a rate of 38,500 ± 900 reactions per minute.

S. wagneri is an obligate anaerobic chemolithoautotroph and undergoes anaerobic ammonium oxidation (anammox) in the intracytoplasmic compartment called an anammoxosome. During the anammox process, ammonium is oxidized using nitrite as an electron acceptor and forms dinitrogen gas as a product. It is proposed that this mechanism occurs through the production of a hydrazine intermediate using hydroxylamine, which is derived from nitrite. In addition, S. wagneri uses nitrite as an electron donor to fix carbon dioxide and forms nitrate as a byproduct.

Strong light causes the reduction of the plastoquinone pool, which leads to protonation and double reduction (and double protonation) of the QA electron acceptor of Photosystem II. The protonated and double-reduced forms of QA do not function in electron transport. Furthermore, charge recombination reactions in inhibited Photosystem II are expected to lead to the triplet state of the primary donor (P680) more probably than same reactions in active PSII. Triplet P680 may react with oxygen to produce harmful singlet oxygen.

Beta-1,3-galactosyltransferase 4 is an enzyme that in humans is encoded by the B3GALT4 gene. This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon.

The most important such solvents are dimethylsulfoxide, DMSO, and acetonitrile, CH3CN, as these solvents have been widely used to measure the acid dissociation constants of organic molecules. Because DMSO is a stronger proton acceptor than H2O the acid becomes a stronger acid in this solvent than in water. Indeed, many molecules behave as acids in non-aqueous solution that do not do so in aqueous solution. An extreme case occurs with carbon acids, where a proton is extracted from a C-H bond.

Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial is an enzyme that in humans is encoded by the IDH3B gene. Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic.

An aryl sulfotransferase () is an enzyme that transfers a sulfate group from phenolic sulfate esters to a phenolic acceptor substrate. :3'-phosphoadenylyl sulfate + a phenol \rightleftharpoons adenosine 3',5'-bisphosphate + an aryl sulfate Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenol, whereas its two products are adenosine 3',5'-bisphosphate and aryl sulfate. These enzymes are transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenol sulfotransferase.

The bacterium is chemolithotrophic and is capable of using nitrate as the terminal electron acceptor in the electron transport chain. The organism will oxidize hydrogen sulfide (H2S) into elemental sulfur (S). This is deposited as granules in its periplasm and is highly refractile and opalescent, making the organism look like a pearl. While the sulfide is available in the surrounding sediment, produced by other bacteria from dead microalgae that sank down to the sea bottom, the nitrate comes from the above seawater.

However, the resistance decreases as the charge carrier density (i.e., without introducing further complications, the density of electrons) in the conduction band increases. In extrinsic (doped) semiconductors, dopant atoms increase the majority charge carrier concentration by donating electrons to the conduction band or producing holes in the valence band. (A "hole" is a position where an electron is missing; such holes can behave in a similar way to electrons.) For both types of donor or acceptor atoms, increasing dopant density reduces resistance.

A pharmacophore model consisting of four hydrogen bond donor sites and three hydrogen bond acceptor sites was proposed for this domain. Unlike the proteinase domain, the ancillary domain varies by ADAMTS protein and includes any number of thrombospondin (TSP) type 1 motifs, one cysteine-rich and spacer domain, and other domains specific to certain ADAMTS proteins. ADAMTS7 in particular possesses 8 TSP type 1 motifs which, together with its spacer domain, participate in the protein’s tight interaction with the extracellular matrix.

Two of homocysteine's main biochemical roles - (Homocysteine is seen in the left middle of the image.) It can be synthesized from methionine and then converted back to methionine via the SAM cycle or used to create cysteine and alpha- ketobutyrate. Homocysteine is biosynthesized naturally via a multi-step process. First, methionine receives an adenosine group from ATP, a reaction catalyzed by S-adenosyl-methionine synthetase, to give S-adenosyl methionine (SAM). SAM then transfers the methyl group to an acceptor molecule, (e.g.

Oxyhemoglobin is formed during physiological respiration when oxygen binds to the heme component of the protein hemoglobin in red blood cells. This process occurs in the pulmonary capillaries adjacent to the alveoli of the lungs. The oxygen then travels through the blood stream to be dropped off at cells where it is utilized as a terminal electron acceptor in the production of ATP by the process of oxidative phosphorylation. It does not, however, help to counteract a decrease in blood pH.

In low oxygen environments, such as oxygen minimum zones and seafloor sediments, chemoorganoheterotrophic microbes use nitrate as an electron acceptor for respiration, reducing it to nitrite, then to ammonium. Since, like nitrification, DNRA alters the balance in the availability of nitrate and ammonium, it has the potential to introduce inaccuracy to the calculated f-ratio. However, as DNRA's occurrence is limited to anaerobic situations, its importance is less widespread than nitrification, although it can occur in association with primary producers.

8: Co-crystals of substituted c-DTTBC and C60.Toluene molecules are shown in green. Planar hetero junction OPV in ball and socket joint model When it comes to the reasons that limit OPVs power conversion efficiencies, we need to understand the structural and chemical limitations that existing organic small molecules offer. The OPVs make use of a pair of electron acceptor fullerene or another non-fullerene (n-type) and electron donor molecules (p-type) creating heterojunctions within the active film.

The comparison of electrostatic surface potentials (ESPs) of aromatic rings in tryptophan, tyrosine, phenylalanine, and histidine suggests that electronic effects also play a role in the binding to glycans (see Figure 2). After normalizing the electron densities for surface area, the tryptophan still remains the most electron rich acceptor of CH-\pi interactions, suggesting a possible reason for its 9-fold prevalence in carbohydrate binding pockets. Overall, the electrostatic potential maps follow the prevalence trend of Trp >> Tyr > (Phe) > His. Figure 2.

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial is an enzyme that in humans is encoded by the IDH3G gene. Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic.

Isocitrate dehydrogenase [NADP], mitochondrial is an enzyme that in humans is encoded by the IDH2 gene. Isocitrate dehydrogenases are enzymes that catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic.

Takahashi et al. (1985) determined that human plasma Hx consists of a single polypeptide chain of 439 amino acids residues with six intrachain disulfide bridges and has a molecular mass of approximately 63 kD. The amino-terminal threonine residue is blocked by an O-linked galactosamine oligosaccharide, and the protein has five glucosamine oligosaccharides N-linked to the acceptor sequence Asn-X-Ser/Thr. The 18 tryptophan residues are arranged in four clusters, and 12 of the tryptophans are conserved in homologous positions.

381(1); 102–115 Hydrogen bonds between the water molecule, which is linked to Ile50 and Ile50', and carbonyl groups of the peptidomimetic inhibitors seem to connect them with the flap regions. On the other hand, on the nonpeptidic inhibitors, there is a proton acceptor which replaces the tetracoordinated water molecule and interacts directly with the two Ile50 residues on the flap of the enzyme.Lebon, F. and Ledecq, M. (2000) Approaches to the Design of Effective HIV-1 Protease Inhibitors. Current Medicinal Chemistry.

Donor-acceptor coupling is weak, both keep their identity during the reaction. Therefore, the electron, being an elementary particle, can only "jump" as a whole (electron transfer, ET). If the electron jumps, the transfer is much faster than the movement of the large solvent molecules, with the consequence that the nuclear positions of the reaction partners and the solvent molecules are the same before and after the electron jump (Franck–Condon principle).W.F. Libby, "Theory of Electron Exchange Reactions in Aqueous Solution" J.Phys.Chem.

Quinate/shikimate dehydrogenase (, YdiB) is an enzyme with systematic name L-quinate:NAD(P)+ 3-oxidoreductase. This enzyme catalyses the following chemical reaction : (1) L-quinate + NAD(P)+ \rightleftharpoons 3-dehydroquinate + NAD(P)H + H+ : (2) shikimate + NAD(P)+ \rightleftharpoons 3-dehydroshikimate + NAD(P)H + H+ This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate dehydrogenase, in that it can use both quinate and shikimate as substrate, and either NAD+ or NADP+ as acceptor.

Beta-1,3-galactosyltransferase 5 is an enzyme that in humans is encoded by the B3GALT5 gene. This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon.

Biochemical basis of mitochondrial acetaldehyde dismutation in Saccharomyces cerevisiae While in respiration electrons are transferred from substrate (electron donor) to an electron acceptor, in fermentation part of the substrate molecule itself accepts the electrons. Fermentation is therefore a type of disproportionation, and does not involve an overall change in oxidation state of the substrate. Most of the fermentative substrates are organic molecules. However, a rare type of fermentation may also involve the disproportionation of inorganic sulfur compounds in certain sulfate-reducing bacteria.

Most well-studied RNA tertiary structures contain examples of coaxial stacking. Some prominent examples are tRNA-Phe, group I introns, group II introns, and ribosomal RNAs. Crystal structures of tRNA revealed the presence of two extended helices that result from coaxial stacking of the amino-acid acceptor stem with the T-arm, and stacking of the D- and anticodon-arms. These interactions within tRNA orient the anticodon stem perpendicularly to the amino-acid stem, leading to the functional L-shaped tertiary structure.

A well- recognized instrument, the Negative Pressure Instrument, from Electronic Diversities, Finksburg MD, US, is used with heated chambers to produce various-sized suction blisters with less time and improved success. The blisters are then cut, emptied and the loose skin is transferred side by side to the non-healing wound. Subsequently, the donor-site is treated with antiseptic drugs and covered with bandages. The acceptor-site is treated with non-adherent bandages, to prevent the skin graft from sticking to the bandages.

The traditional method for attaching sugars to natural products, drugs or drug leads is by chemical glycosylation. This classical approach typically requires multiple protection/deprotection steps in addition to the key anomeric activation/coupling reaction which, depending upon the glycosyl donor/acceptor pair, can lead to a mixture of anomers. Unlike classical chemical glycosylation, glycorandomization methods are divergent (i.e., diverge from a common starting material, see divergent synthesis) and are not dependent upon sugar/aglycon protection/deprotection or sugar anomeric activation.

The phosphasilene Si=P double bond is highly reactive, yet with the choice of proper substituents, it can be stabilized via donor-acceptor interaction or by steric congestion.146x146px The landmark discovery of the first phosphasilene by NMR spectroscopy was made in 1984 by Bickelhaupt et al. The first phosphasilene came with bulky aryl substituents at the phosphorus and silicon atoms. Almost a decade after this spectroscopic observation, the first structural characterization of phosphasilene was achieved in 1993 by Niecke et al.

The primary donor receives excitation energy either by absorbing a photon of suitable frequency (colour) or by excitation energy transfer from other chlorophylls within photosystem II. During excitation, an electron is excited to a higher energy level. This electron is subsequently captured by the primary electron acceptor, a pheophytin molecule located within photosystem II near P680. The oxidized P680 (P680+) is subsequently reduced by an electron originating from water (via Oxygen evolving complex). Oxidized P680 (P680+) is the strongest biological oxidizing agent known.

In this method, the glycosyl donor is protected at the C-2 position by an OAc group. The C-2-OAc protecting group is transformed into an enol ether by the Tebbe reagent (Cp2Ti=CH2), and then the glycosyl acceptor is tethered to the enol ether under acid-catalysed conditions to generate a mixed acetal. In a subsequent step, the β-mannoside is formed upon activation of the anomeric leaving group (Y), followed by work up.Barresi, F.; Hindsgaul, O. J. Am. Chem. Soc.

Sulfolobus proteins are of interest for biotechnology and industrial use due to their thermostable nature. One application is the creation of artificial derivatives from S. acidocaldarius proteins, named affitins. Intracellular proteins are not necessarily stable at low pH however, as Sulfolobus species maintain a significant pH gradient across the outer membrane. Sulfolobales are metabolically dependent on sulfur: heterotrophic or autotrophic, their energy comes from the oxidation of sulfur and/or cellular respiration in which sulfur acts as the final electron acceptor.

The transition of iron between Fe(II) and Fe(III) in aquatic systems interacts with the freshwater phosphorus cycle. With oxygen in the water, Fe(II) gets oxidized to Fe(III), either abiotically or by microbes via lithotrophic oxidation. Fe(III) can form iron hydroxides, which bind tightly to phosphorus, removing it from the bioavailable phosphorus pool, limiting primary productivity. In anoxic conditions, Fe(III) can reduced, used by microbes to be the final electron acceptor from either organic carbon or H2.

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

In enzymology, a geissoschizine dehydrogenase () is an enzyme that catalyzes the chemical reaction :geissoschizine + NADP+ \rightleftharpoons 4,21-didehydrogeissoschizine + NADPH Thus, the two substrates of this enzyme are geissoschizine and NADP+, whereas its two products are 4,21-didehydrogeissoschizine and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is geissoschizine:NADP+ 4,21-oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a phloroglucinol reductase () is an enzyme that catalyzes the chemical reaction :dihydrophloroglucinol + NADP+ \rightleftharpoons phloroglucinol + NADPH + H+ Thus, the two substrates of this enzyme are dihydrophloroglucinol and NADP+, whereas its 3 products are phloroglucinol, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrophloroglucinol:NADP+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.

Structure of Crotonyl CoA carboxylase/reductase. From Streptomycs collinus.; ; rendered using PyMOL. In enzymology, an acyl-CoA dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :acyl-CoA + NADP+ \rightleftharpoons 2,3-dehydroacyl-CoA + NADPH + H+ Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor.

In enzymology, a bilirubin oxidase, BOD or BOx, () is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction :2 bilirubin + O2 \rightleftharpoons 2 biliverdin + 2 H2O This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism.

The simplest organic PV device features a planar heterojunction (Fig. 1). A film of organic active material (polymer or small molecule), of electron donor or electron acceptor type is sandwiched between contacts. Excitons created in the active material may diffuse before recombining and separate, hole and electron diffusing to its specific collecting electrode. Because charge carriers have diffusion lengths of just 3–10 nm in typical amorphous organic semiconductors, planar cells must be thin, but the thin cells absorb light less well.

Transactions are any action that has a monetary implication or transfer information from one media to another. The most commonly thought of transactions are the use of credit or debit cards through a card reader of some type. Card readers are also widely used for hotel door locks or access control devices. Another of the most common is a currency transaction via vending, slot machines, or self-checkout kiosk where a bill acceptor takes currency or a currency detector tabulates quantity.

Since the organism is a strict aerobe, it used oxygen as a terminal electron acceptor. The organism can grow on peptone and tryptone as the sole carbon and nitrogen sources. D. donghaensis cannot grow in the absence of NaCl or when it is greater than 7% (w/v); growth is optimal at 2% (w/v) NaCl. The organism is susceptible to the antibiotics tetracycline and carbenicillin, although the organism's ability to form biofilms makes it difficult for antibiotics to penetrate the viscous layers.

The bioluminescence produced is not bright enough to serve as indoor lighting, however, streetlights do not need to be very bright to serve their function. Vibrio bacteria are oxidase positive facultative anaerobes Oxidase positive bacteria can use oxygen as the final electron acceptor in the electron transport chain. Facultative anaerobes can use oxygen or they can use fermentation to generate ATP. Lights made with V. azasii would be able to use oxygen freely without the need to create an anaerobic chamber.

Another use of methylene blue is to treat ifosfamide neurotoxicity. Methylene blue was first reported for treatment and prophylaxis of ifosfamide neuropsychiatric toxicity in 1994. A toxic metabolite of ifosfamide, chloroacetaldehyde (CAA), disrupts the mitochondrial respiratory chain, leading to an accumulation of nicotinamide adenine dinucleotide hydrogen (NADH). Methylene blue acts as an alternative electron acceptor, and reverses the NADH inhibition of hepatic gluconeogenesis while also inhibiting the transformation of chloroethylamine into chloroacetaldehyde, and inhibits multiple amine oxidase activities, preventing the formation of CAA.

In enzymology, a rifamycin-B oxidase () is an enzyme that catalyzes the chemical reaction :rifamycin B + O2 \rightleftharpoons rifamycin O + H2O2 Thus, the two substrates of this enzyme are rifamycin B and O2, whereas its two products are rifamycin O and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. The systematic name of this enzyme class is rifamycin-B:oxygen oxidoreductase. This enzyme is also called rifamycin B oxidase.

JH diol kinase: part II- Sequencing, cloning, and molecular modeling of juvenile hormone-selective diol kinase from Manduca sexta. J. Biol. Chem. 277, 21882–21890 The specificity of JHDK for JH I diol is relatively high, considering the multitude of potential phosphate acceptor groups present in a cell. The enzyme does not recognize methyl geranoate diol (one isoprenyl unit shorter than JH) nor methyl geranylgeranoate diol (one isoprenyl group longer than JH), yet it does recognize JH I ethyl ester diol.

In enzymology, a glutathione—homocystine transhydrogenase () is an enzyme that catalyzes the chemical reaction :2 glutathione + homocystine \rightleftharpoons glutathione disulfide + 2 homocysteine Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two products are glutathione disulfide and homocysteine. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. This enzyme participates in methionine metabolism and glutathione metabolism.

Glycine decarboxylase () is an enzyme that catalyzes the following chemical reaction: :glycine + H-protein-lipoyllysine \rightleftharpoons H-protein-S-aminomethyldihydrolipoyllysine + CO2 Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

In enzymology, a hyponitrite reductase is an enzyme that catalyzes the oxidation of hydroxylamine by the nicotinamide adenine dinucleotide cation (NAD+) into hyponitrous acid HON=NOH: :2 + 2 NAD+ \rightleftharpoons HON=NOH + 2 NADH + 2 H+ This systematic name of this enzyme class hydroxylamine:NAD+ oxidoreductase. It is also called NADH2:hyponitrite oxidoreductase. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor. It employs one cofactor, metal.

Alanopine dehydrogenase () is an enzyme that catalyzes the chemical reaction :2,2'-iminodipropanoate + NAD+ \+ H2O \rightleftharpoons L-alanine + pyruvate + NADH + H+ The 2 substrates of this enzyme are 2,2'-iminodipropanoate, and nicotinamide adenine dinucleotide+. water is excluded since water is 55M and does not change. Its 4 products are L-alanine, pyruvate, nicotinamide adenine dinucleotide, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor.

In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen. This enzyme belongs to oxidoreductases, specifically those acting on the CH- NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta- alanine metabolism, and alkaloid biosynthesis ii.

In enzymology, an ethanolamine oxidase () is an enzyme that catalyzes the chemical reaction :ethanolamine + H2O + O2 \rightleftharpoons glycolaldehyde + NH3 \+ H2O2 The 3 substrates of this enzyme are ethanolamine, H2O, and O2, whereas its 3 products are glycolaldehyde, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is ethanolamine:oxygen oxidoreductase (deaminating). It has 2 cofactors: cobalt, and Cobamide.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase. Other names in common use include 6,7-dihydropteridine:NAD(P)H oxidoreductase, DHPR, NAD(P)H:6,7-dihydropteridine oxidoreductase, NADH-dihydropteridine reductase, NADPH-dihydropteridine reductase, NADPH-specific dihydropteridine reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide), reductase, dihydropteridine reductase, dihydropteridine reductase (NADH), and 5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase.

Kinase is a large family of enzymes that are responsible for catalyzing the transfer of a phosphoryl group from a nucleoside triphosphate donor, such as ATP, to an acceptor molecule. Tyrosine kinases catalyze the phosphorylation of tyrosine residues in proteins. The phosphorylation of tyrosine residues in turn causes a change in the function of the protein that they are contained in. Phosphorylation at tyrosine residues controls a wide range of properties in proteins such as enzyme activity, subcellular localization, and interaction between molecules.

In enzymology, a retinal oxidase () is an enzyme that catalyzes the chemical reaction :retinal + O2 \+ H2O \rightleftharpoons retinoic acid + H2O2 The 3 substrates of this enzyme are retinal, O2, and H2O, whereas its two products are retinoic acid and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is retinal:oxygen oxidoreductase. This enzyme is also called retinene oxidase.

In enzymology, a vanillin dehydrogenase () is an enzyme that catalyzes the chemical reaction :100px + NAD+ \+ H2O \rightleftharpoons 100px + NADH + H+ The 3 substrates of this enzyme are vanillin, NAD+, and H2O, whereas its 3 products are vanillate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vanillin:NAD+ oxidoreductase. This enzyme participates in 2,4-dichlorobenzoate degradation.

Depending on attached accessory proteins (A,B,C,D-Clusters), serve a variety of catalytic functions, including reduction of [4Fe-4S] clusters and insertion of nickel. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include anaerobic carbon monoxide dehydrogenase, carbon monoxide oxygenase, carbon-monoxide dehydrogenase, and carbon-monoxide:(acceptor) oxidoreductase.

In enzymology, an aryl-aldehyde oxidase () is an enzyme that catalyzes the chemical reaction :an aromatic aldehyde + O2 \+ H2O \rightleftharpoons an aromatic carboxylic acid + H2O2 The 3 substrates of this enzyme are aromatic aldehyde, O2, and H2O, whereas its two products are aromatic carboxylic acid and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is aryl-aldehyde:oxygen oxidoreductase.

In enzymology, an alcohol oxidase () is an enzyme that catalyzes the chemical reaction :a primary alcohol + O2 \rightleftharpoons an aldehyde + H2O2 Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as the acceptor. The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase.

In enzymology, a catechol oxidase (dimerizing) () is an enzyme that catalyzes the chemical reaction :4 catechol + 3 O2 \rightleftharpoons 2 dibenzo[1,4]dioxin-2,3-dione + 6 H2O Thus, the two substrates of this enzyme are catechol and O2, whereas its two products are dibenzo[1,4]dioxin-2,3-dione and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is catechol:oxygen oxidoreductase (dimerizing).

In enzymology, a vanillyl-alcohol oxidase () is an enzyme that catalyzes the chemical reaction :110px + O2 \rightleftharpoons 115px + H2O2 Thus, the two substrates of this enzyme are vanillyl alcohol and O2, whereas its two products are vanillin and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2-methoxybenzyl alcohol oxidase.

In enzymology, a L-sorbose oxidase () is an enzyme that catalyzes the chemical reaction :L-sorbose + O2 \rightleftharpoons 5-dehydro-D-fructose + H2O2 Thus, the two substrates of this enzyme are L-sorbose and O2, whereas its two products are 5-dehydro-D-fructose and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is L-sorbose:oxygen 5-oxidoreductase.

In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) () is an enzyme that catalyzes the chemical reaction :CO + H2O + oxidized ferredoxin \rightleftharpoons CO2 \+ reduced ferredoxin The 3 substrates of this enzyme are CO, H2O, and oxidized ferredoxin, whereas its two products are CO2 and reduced ferredoxin. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron- sulfur protein as acceptor. The systematic name of this enzyme class is carbon-monoxide,water:ferredoxin oxidoreductase.

In enzymology, a choline oxidase () is an enzyme that catalyzes the chemical reaction :choline + O2 \rightleftharpoons betaine aldehyde + H2O2 Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism.

In enzymology, a -mannitol oxidase () is an enzyme that catalyzes the chemical reaction :mannitol + O2 \rightleftharpoons mannose + H2O2 Thus, the two substrates of this enzyme are mannitol and O2, whereas its two products are mannose and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is mannitol:oxygen oxidoreductase (cyclizing). Other names in common use include mannitol oxidase, and D-arabitol oxidase.

Lead(II) is a hard acceptor; it forms stronger complexes with nitrogen and oxygen electron-donating ligands. For example, combining lead nitrate and pentaethylene glycol (EO5) in a solution of acetonitrile and methanol followed by slow evaporation produced the compound [Pb(NO3)2(EO5)]. In the crystal structure for this compound, the EO5 chain is wrapped around the lead ion in an equatorial plane similar to that of a crown ether. The two bidentate nitrate ligands are in trans configuration.

FNR utilizes FAD, which can exist in an oxidized state, single electron reduced semiquinone state, and fully reduced state to mediate this electron transfer. FNR has an induced-fit mechanism of catalysis. Binding of ferredoxin to the enzyme causes the formation of a hydrogen bond between a glutamate residue (E312) and a serine residue (S96) in the active site. The glutamate residue is highly conserved because it both stabilizes the semiquinone form of FAD and is a proton donor/acceptor in the reaction.

In enzymology, a pteridine oxidase () is an enzyme that catalyzes the chemical reaction :2-amino-4-hydroxypteridine + O2 \rightleftharpoons 2-amino-4,7-dihydroxypteridine + (?) Thus, the two substrates of this enzyme are 2-amino-4-hydroxypteridine and O2, whereas its product is 2-amino-4,7-dihydroxypteridine. This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with oxygen as acceptor. The systematic name of this enzyme class is 2-amino-4-hydroxypteridine:oxygen oxidoreductase (7-hydroxylating).

In enzymology, a fatty-acid peroxidase () is an enzyme that catalyzes the chemical reaction :palmitate + 2 H2O2 \rightleftharpoons pentadecanal + CO2 \+ 3 H2O Thus, the two substrates of this enzyme are palmitate and H2O2, whereas its 3 products are pentadecanal, CO2, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is hexadecanoate:hydrogen-peroxide oxidoreductase. This enzyme is also called long chain fatty acid peroxidase.

In enzymology, a methylarsonate reductase () is an enzyme that catalyzes the chemical reaction :methylarsonate + 2 glutathione \rightleftharpoons methylarsonite + glutathione disulfide + H2O Thus, the two substrates of this enzyme are methylarsonate and glutathione, whereas its 3 products are methylarsonite, glutathione disulfide, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with disulfide as acceptor. The systematic name of this enzyme class is gluthathione:methylarsonate oxidoreductase. This enzyme is also called MMA(V) reductase.

In enzymology, a mycothione reductase () is an enzyme that catalyzes the chemical reaction :mycothione + NAD(P)H + H + \rightleftharpoons 2 mycothiol + NADP+ in M. tuberculosis and other actinomycetes. The 2 substrates of this enzyme are mycothiol and NADPH, whereas 2 molecules of mycothione and NADP+ are formed as products. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is mycothiol:NAD(P)+ oxidoreductase.

In enzymology, a p-benzoquinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :NADPH + H+ \+ p-benzoquinone \rightleftharpoons NADP+ \+ hydroquinone The 3 substrates of this enzyme are NADPH, H+, and p-benzoquinone, whereas its two products are NADP+ and hydroquinone. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a quinone or similar compound as acceptor. The systematic name of this enzyme class is NADPH:p-benzoquinone oxidoreductase. This enzyme participates in gamma-hexachlorocyclohexane degradation.

Stearoyl-CoA desaturase-1 is a key enzyme in fatty acid metabolism. It is responsible for forming a double bond in Stearoyl-CoA. This is how the monounsaturated fatty acid oleic acid is produced from the saturated fatty acid stearic acid. A series of redox reactions, during which two electrons flow from NADH to flavoprotein cytochrome b5, then to the electron acceptor cytochrome b5 as well as molecular oxygen introduces a single double bond within a row of methylene fatty acyl-CoA substrates.

Trimethyl phosphite is prepared from phosphorus trichloride: :PCl3 \+ 3 CH3OH → P(OCH3)3 \+ 3 HCl It is susceptible to oxidation to trimethyl phosphate. It reacts with a catalytic amount of methyl iodide in the Arbuzov reaction to give dimethyl methylphosphonate: :P(OCH3)3 → CH3P(O)(OCH3)2 As a ligand, trimethyl phosphite has a smaller cone angle and better acceptor properties relative to trimethylphosphine. A representative derivative is the colorless tetrahedral complex Ni(P(OMe)3)4 (m.p. 108 °C).

The donor and/or acceptor compartments may contain solubilizing agents, or additives that bind the drugs as they permeate. To improve the in vitro - in vivo correlation and performance of the PAMPA method, the lipid, pH and chemical composition of the system is often designed with biomimetic considerations in mind. Although active transport is not modeled by the artificial PAMPA membrane, up to 95% of known drugs are absorbed by passive transport.Artursson, P. Application of physicochemical properties of molecules to predict intestinal permeability.

A glycosyl donor is a carbohydrate mono- or oligosaccharide that will react with a suitable glycosyl acceptor to form a new glycosidic bond. By convention, the donor is the member of this pair that contains the resulting anomeric carbon of the new glycosidic bond.T. K. Lindhorst "Essentials of Carbohydrate Chemistry and Biochemistry" 2007 Wiley-VCH Verlag, Weinheim The resulting reaction is referred to as a glycosylation or chemical glycosylation. In a glycosyl donor, a leaving group is required at the anomeric position.

In enzymology, an erythrulose reductase () is an enzyme that catalyzes the chemical reaction :erythritol + NADP+ \rightleftharpoons D-erythrulose + NADPH + H+ Thus, the two substrates of this enzyme are erythritol and NADP+, whereas its 3 products are D-erythrulose, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is erythritol:NADP+ oxidoreductase. This enzyme is also called D-erythrulose reductase.

In enzymology, a chlordecone reductase () is an enzyme that catalyzes the chemical reaction :chlordecone alcohol + NADP+ \rightleftharpoons chlordecone + NADPH + H+ Thus, the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR.

In enzymology, a codeinone reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :codeine + NADP+ \rightleftharpoons codeinone + NADPH + H+ Thus, the two substrates of this enzyme are codeine and NADP+, whereas its 3 products are codeinone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is codeine:NADP+ oxidoreductase. This enzyme participates in alkaloid biosynthesis i.

In enzymology, an isopiperitenol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(-)-trans-isopiperitenol + NAD+ \rightleftharpoons (-)-isopiperitenone + NADH + H+ Thus, the two substrates of this enzyme are (-)-trans-isopiperitenol and NAD+, whereas its 3 products are (-)-isopiperitenone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-trans-isopiperitenol:NAD+ oxidoreductase. This enzyme participates in monoterpenoid biosynthesis.

In enzymology, a serine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-serine + NADP+ \rightleftharpoons 2-ammoniomalonate semialdehyde + NADPH + H+ Thus, the two substrates of this enzyme are L-serine and NADP+, whereas its 3 products are 2-ammoniomalonate semialdehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-serine:NADP+ 3-oxidoreductase.

In enzymology, a taurocyamine kinase () is an enzyme that catalyzes the chemical reaction :ATP + taurocyamine \rightleftharpoons ADP + N-phosphotaurocyamine Thus, the two substrates of this enzyme are ATP and taurocyamine, whereas its two products are ADP and N-phosphotaurocyamine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:taurocyamine N-phosphotransferase. Other names in common use include taurocyamine phosphotransferase, and ATP:taurocyamine phosphotransferase.

In enzymology, a pantetheine kinase () is an enzyme that catalyzes the chemical reaction :ATP + pantetheine \rightleftharpoons ADP + pantetheine 4'-phosphate Thus, the two substrates of this enzyme are ATP and pantetheine, whereas its two products are ADP and pantetheine 4'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pantetheine 4'-phosphotransferase. This enzyme is also called pantetheine kinase (phosphorylating).

In enzymology, a pseudouridine kinase () is an enzyme that catalyzes the chemical reaction :ATP + pseudouridine \rightleftharpoons ADP + pseudouridine 5'-phosphate Thus, the two substrates of this enzyme are ATP and pseudouridine, whereas its two products are ADP and pseudouridine 5'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:pseudouridine 5'-phosphotransferase. This enzyme is also called pseudouridine kinase (phosphorylating).

In enzymology, a sedoheptulokinase () is an enzyme that catalyzes the chemical reaction :ATP + sedoheptulose \rightleftharpoons ADP + sedoheptulose 7-phosphate Thus, the two substrates of this enzyme are ATP and sedoheptulose, whereas its two products are ADP and sedoheptulose 7-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:sedoheptulose 7-phosphotransferase. Other names in common use include heptulokinase, and sedoheptulokinase (phosphorylating).

In enzymology, a ribosylnicotinamide kinase () is an enzyme that catalyzes the chemical reaction :ATP + N-ribosylnicotinamide \rightleftharpoons ADP + nicotinamide ribonucleotide Thus, the two substrates of this enzyme are ATP and N-ribosylnicotinamide, whereas its two products are ADP and nicotinamide ribonucleotide. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:N-ribosylnicotinamide 5'-phosphotransferase. This enzyme is also called ribosylnicotinamide kinase (phosphorylating).

In enzymology, viomycin kinase () is an enzyme that catalyzes the chemical reaction :ATP + viomycin \rightleftharpoons ADP + O-phosphoviomycin Thus, the two substrates of this enzyme are ATP and viomycin, whereas its two products are ADP and O-phosphoviomycin. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:viomycin O-phosphotransferase. Other names in common use include viomycin phosphotransferase, and capreomycin phosphotransferase.

In enzymology, a 3alpha-hydroxyglycyrrhetinate dehydrogenase () is an enzyme that catalyzes the chemical reaction :3alpha-hydroxyglycyrrhetinate + NADP+ \rightleftharpoons 3-oxoglycyrrhetinate + NADPH + H+ Thus, the two substrates of this enzyme are 3alpha-hydroxyglycyrrhetinate and NADP+, whereas its 3 products are 3-oxoglycyrrhetinate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3alpha-hydroxyglycyrrhetinate:NADP+ 3-oxidoreductase.

In enzymology, an ethanolamine kinase () is an enzyme that catalyzes the chemical reaction :ATP + ethanolamine \rightleftharpoons ADP + O-phosphoethanolamine Thus, the two substrates of this enzyme are ATP and ethanolamine, whereas its two products are ADP and O-phosphoethanolamine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ethanolamine O-phosphotransferase. Other names in common use include ethanolamine kinase (phosphorylating), and ethanolamine phosphokinase.

In enzymology, a farnesyl-diphosphate kinase () is an enzyme that catalyzes the chemical reaction :ATP + farnesyl diphosphate \rightleftharpoons ADP + farnesyl triphosphate Thus, the two substrates of this enzyme are ATP and farnesyl diphosphate, whereas its two products are ADP and farnesyl triphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:farnesyl-diphosphate phosphotransferase. This enzyme is also called farnesyl pyrophosphate kinase.

In enzymology, a dolichol kinase () is an enzyme that catalyzes the chemical reaction :CTP + dolichol \rightleftharpoons CDP + dolichyl phosphate Thus, the two substrates of this enzyme are CTP and dolichol, whereas its two products are CDP and dolichyl phosphate. This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase.

In enzymology, an erythritol kinase () is an enzyme that catalyzes the chemical reaction :ATP + erythritol \rightleftharpoons ADP + D-erythritol 4-phosphate Thus, the two substrates of this enzyme are ATP and erythritol, whereas its two products are ADP and D-erythritol 4-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:erythritol 4-phosphotransferase. This enzyme is also called erythritol kinase (phosphorylating).

In enzymology, a (S)-carnitine 3-dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-carnitine + NAD \rightleftharpoons 3-dehydrocarnitine + NADH + H Thus, the two substrates of this enzyme are (S)-carnitine and NAD, whereas its 3 products are 3-dehydrocarnitine, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (S)-carnitine:NAD oxidoreductase.

In enzymology, a salutaridine reductase (NADPH) () is an enzyme that catalyzes the chemical reaction :salutaridinol + NADP+ \rightleftharpoons salutaridine + NADPH + H+ Thus, the two substrates of this enzyme are salutaridinol and NADP+, whereas its 3 products are salutaridine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salutaridinol:NADP+ 7-oxidoreductase. This enzyme participates in alkaloid biosynthesis i.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D- gluconate:NAD+ 5-oxidoreductase. Other names in common use include 2-keto-3-deoxygluconate 5-dehydrogenase, 2-keto-3-deoxy-D-gluconate dehydrogenase, 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide, (phosphate)) dehydrogenase, 2-keto-3-deoxy-D-gluconate (3-deoxy-D- glycero-2,5-hexodiulosonic, and acid) dehydrogenase.

In enzymology, a mevaldate reductase () is an enzyme that catalyzes the chemical reaction :(R)-mevalonate + NAD+ \rightleftharpoons mevaldate + NADH + H+ Thus, the two substrates of this enzyme are (R)-mevalonate and NAD+, whereas its 3 products are mevaldate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-mevalonate:NAD+ oxidoreductase. This enzyme is also called mevalonic dehydrogenase.

In enzymology, a carbamate kinase () is an enzyme that catalyzes the chemical reaction :ATP + NH3 \+ CO2 \rightleftharpoons ADP + carbamoyl phosphate The 3 substrates of this enzyme are ATP, NH3, and CO2, whereas its two products are ADP and carbamoyl phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:carbamate phosphotransferase. Other names in common use include CKase, carbamoyl phosphokinase, and carbamyl phosphokinase.

In enzymology, an ammonia kinase () is an enzyme that catalyzes the chemical reaction :ATP + NH3 \rightleftharpoons ADP + phosphoramide Thus, the two substrates of this enzyme are ATP and NH3, whereas its two products are ADP and phosphoramide. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:ammonia phosphotransferase. Other names in common use include phosphoramidate-adenosine diphosphate phosphotransferase, and phosphoramidate-ADP-phosphotransferase.

In enzymology, an AMP—thymidine kinase () is an enzyme that catalyzes the chemical reaction :AMP + thymidine \rightleftharpoons adenosine + thymidine 5'-phosphate Thus, the two substrates of this enzyme are AMP and thymidine, whereas its two products are adenosine and thymidine 5'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is AMP:thymidine 5'-phosphotransferase. This enzyme is also called adenylate-nucleoside phosphotransferase.

The association of phosphorylation and the reduction of an electron acceptor such as ferricyanide increase similarly with the addition of phosphate, magnesium (Mg), and ADP. The existence of these three components is important for maximal reductive and phosphorylative activity. Similar increases in the rate of ferricyanide reduction can be stimulated by a dilution technique. Dilution does not cause a further increase in the rate in which ferricyanide is reduced with the accumulation of ADP, phosphate, and Mg to a treated chloroplast suspension.

Although it is not as problematic as benzopyrene, animal studies have shown pyrene is toxic to the kidneys and liver. It is now known that pyrene affects several living functions in fish and algae. Experiments in pigs show that urinary 1-hydroxypyrene is a metabolite of pyrene, when given orally. Pyrenes are strong electron donor materials and can be combined with several materials in order to make electron donor-acceptor systems which can be used in energy conversion and light harvesting applications.

In the process, ATP is recovered and oxygen molecules serve as the final electron acceptor in the reaction, leading to the lowering of ambient oxygen levels. This is to the benefit of the nitrogenases, which only function anaerobically. As a result of their mutually beneficial relationship with Frankia, alder trees improve the fertility of the soils in which they grow and are considered to be a pioneer species, making the soil more fertile and thus enabling other successional species to become established.

She noted that the methylene blue dye used in the experiment was not reduced. This observation indicated that the tyramine oxidase system, unlike other enzyme systems, was not able to use the dye as a hydrogen acceptor. Additionally, the oxidative process within this enzyme system was seen to be resistant to the addition of cyanide. This observation showed that the tyramine oxidase system was an exception to Warburg's statement, which claimed that direct oxidation could not occur unless atmospheric oxygen was activated by iron.

An interrupted gene (also called a split gene) is a gene that contains expressed regions of DNA called exons, split with unexpressed regions called introns (also called intervening regions). Exons provide instructions for coding proteins, which create mRNA necessary for the synthesis of proteins. Introns are removed by recognition of the donor site (5' end) and the splice acceptor site (3' end). The architecture of the interrupted gene allows for the process of alternative splicing, where various mRNA products can be produced from a single gene.

Crotonyl-CoA reductase (, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction : butanoyl-CoA + NADP+ \rightleftharpoons (E)-but-2-enoyl-CoA + NADPH + H+ This enzyme catalyses the reaction in the reverse direction.

The electron acceptor NAD+ is regenerated from NADH formed in oxidative steps of the fermentation pathway by the reduction of oxidized compounds. These oxidized compounds are often formed during the fermentation pathway itself, but may also be external. For example, in homofermentative lactic acid bacteria, NADH formed during the oxidation of glyceraldehyde-3-phosphate is oxidized back to NAD+ by the reduction of pyruvate to lactic acid at a later stage in the pathway. In yeast, acetaldehyde is reduced to ethanol to regenerate NAD+.

RNase P is now being studied as a potential therapy for diseases such as herpes simplex virus, cytomegalovirus, influenza and other respiratory infections, HIV-1 and cancer caused by fusion gene BCR- ABL. External guide sequences (EGSs) are formed with complementarity to viral or oncogenic mRNA and structures that mimic the T loop and acceptor stem of tRNA. These structures allow RNase P to recognize the EGS and cleave the target mRNA. EGS therapies have shown to be effective in culture and in live mice.

In some bacteria HPr is a domain in a larger protein that includes an EIII(Fru) (IIA) domain and in some cases also an EI domain. There is a conserved histidine in the N-terminus of HPr, which serves as an acceptor for the phosphoryl group of EI. In the central part of HPr there is a conserved serine which, in Gram- positive bacteria only, is phosphorylated by an ATP-dependent protein kinase, a process which probably plays a regulatory role in sugar transport.

Upon treatment with base, this water adduct [Ge[15]crown-5·OH2]2+can be deprotonated to give the hydroxide adduct [Ge[15]crown-5·OH]+. Upon deprotonation to give the hydroxide adduct, the Ge-O bond becomes shorter and stronger. NBO analysis identifies the H2O-Ge[15]crown-5 interaction as a donor-acceptor interaction, while the HO-Ge[15]crown-5 interaction is identified as a polar single bond. This reactivity presents a potential strategy for the preparation of new Ge complexes.

Currently, research in the area of sustainable energy is investigating the application and design of microbial fuel cells (MFC) using R. ferrireducens. In an MFC, a bacterial suspension is provided a reduced compound, which the bacteria use as a source of electrons. The bacteria metabolize this compound and shuttle the released electrons through their respiratory networks and ultimately donate them to a synthetic electron acceptor, also known as an anode. When connected to a cathode, the bacterial metabolism of the reduced compound generates electricity and CO2.

FRET in lanthanide probes is a widely used technique to measure the distance between two points separated by approximately 15–100 Angstrom. Measurements can be done under physiological conditions in vitro with genetically encoded dyes, and often in vivo as well. The technique relies on a distant- dependent transfer of energy from a donor fluorophore to an acceptor dye. Lanthanide probes has been used to study DNA- protein interactions (using a terbium chelate complex) to measure distances in DNA complexes bent by the CAP protein.

Bioremediation is a process used to treat contaminated media, including water, soil and subsurface material, by altering environmental conditions to stimulate growth of microorganisms and degrade the target pollutants. In many cases, bioremediation is less expensive and more sustainable than other remediation alternatives. Biological treatment is a similar approach used to treat wastes including wastewater, industrial waste and solid waste. Most bioremediation processes involve oxidation-reduction reactions where either an electron acceptor (commonly oxygen) is added to stimulate oxidation of a reduced pollutant (e.g.

In compounds like CH3Li with some degree of covalency, bonding is achieved primarily with the 2s orbital, with some contribution from a 2p orbital. (This bonding scheme is used in condensed phase aggregates like (CH3Li)4 as well, leading to a higher coordination number for lithium.) Thus, in principle, up to an octet can be accommodated. Nevertheless, the formal number of valence electrons around Li never exceeds two, unless weak donor-acceptor interactions with neutral ligands (e.g., solvent molecules, often omitted from Lewis structures) are included.

Certain strains cannot use PCE or TCE as electron acceptors (e.g. CBDB1) and some cannot use vinyl chloride as an electron acceptor (e.g. FL2). D. mccartyi strains 195 and SFB93 are inhibited by high concentrations of acetylene (which builds up in contaminated groundwater sites as a result of TCE degradation) via changes in gene expression that likely disrupt normal electron transport chain function. When selecting Dehalococcoides strains for bioremediation use, it is important to consider their metabolic capabilities and their sensitivities to different chemicals.

Tentatively, there may be examples of syntrophy between acidophilic species, and even cross- domain cooperation between archaea and bacteria. One mutalistic example is the rotation of iron between species; ferrous-oxidising chemolithotrophs use iron as an electron donor, then ferric-reducing heterotrophs use iron as an electron-acceptor. Another more synergistic behaviour is the faster oxidation of ferrous iron when A.ferrooxidans and Sulfobacillus thermosulfidooxidans are combined in low-CO2 culture. S.thermosulfidooxidans is a more efficient iron- oxidiser, but this is usually inhibited by low-CO2 uptake.

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (IDH3α) is an enzyme that in humans is encoded by the IDH3A gene. Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic.

Brønsted and Lowry characterized an acid–base equilibrium as involving a proton exchange reaction: Includes discussion of many organic Brønsted acids. Chapter 5: Acids and Bases Chapter 6: Acids, Bases and Ions in Aqueous Solution :acid + base conjugate base + conjugate acid. An acid is a proton donor; the proton is transferred to the base, a proton acceptor, creating a conjugate acid. For aqueous solutions of an acid HA, the base is water; the conjugate base is A− and the conjugate acid is the solvated hydrogen ion.

Aspartate 253 accepts the proton released by the Schiff base (t(1/2) = 10 μs), with the latter being reprotonated by aspartic acid 156 (t(1/2) = 2 ms). The internal proton acceptor and donor groups, corresponding to D212 and D115 in bacteriorhodopsin, are clearly different from other microbial rhodopsins, indicating that their spatial positions in the protein were relocated during evolution. E90 deprotonates exclusively in the nonconductive state. The observed proton transfer reactions and the protein conformational changes relate to the gating of the cation channel.

UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B3GALNT1 gene. This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylgalactosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon.

Alu element copy number differences can be used to distinguish between and construct phylogenies of primate species. Canines differ primarily in their abundance of SINEC_Cf repeats throughout the genome, rather than other gene or allele level mutations. These dog-specific SINEs may code for a splice acceptor site, altering the sequences that appear as exons or introns in each species. Apart from mammals, SINEs can reach high copy numbers in a range of species, including nonbony vertebrates (elephant shark) and some fish species (coelacanths).

Accumulibacter has been shown to remove phosphorus from EBPR plants in Australia, Europe and the USA. It can consume a range of carbon compounds, such as acetate and propionate, under anaerobic conditions and store these compounds as polyhydroxyalkanoates (PHA) which it consumes as a carbon and energy source for growth using oxygen or nitrate as electron acceptor. Recently, another PAO related to the Actinobacteria has been identified in wastewater treatment plants. These organisms appear to be limited to certain amino acids as carbon and energy source.

Denitrifying bacteria are a diverse group of bacteria that encompass many different phyla. This group of bacteria, together with denitrifying fungi and archaea, is capable of performing denitrification as part of the nitrogen cycle. Denitrification is performed by a variety of denitrifying bacteria that are widely distributed in soils and sediments and that utilize oxidized nitrogen compounds in absence of oxygen as a terminal electron acceptor. They metabolise nitrogenous compounds using various enzymes, turning nitrogen oxides back to nitrogen gas (N2) or nitrous oxide (N2O).

It is also the basis of organic solar cells (OSCs), in which the active element is an electron donor, and an electron acceptor material is combined in a bilayer or a bulk heterojunction. Doping with strong electron donor or acceptors can render organic solids conductive even in the absence of light. Examples are doped polyacetylene and doped light-emitting diodes. Today organic semiconductors are used as active elements in organic light- emitting diodes (OLEDs), organic solar cells (OSCs) and organic field-effect transistors (OFETs).

Enzymatic reaction catalyzed by NDH-2. In yellow is represented the protein surface, sitting in the membrane (in gray) NDH-2, also known as type II NADH:quinone oxidoreductase or alternative NADH dehydrogenase, is an enzyme (EC: 1.6.99.3) which catalyzes the electron transfer from NADH (electron donor) to a quinone (electron acceptor), being part of the electron transport chain.B.C. Marreiros, F. Calisto, P.J. Castro, A.M. Duarte, F. V. Sena, A.F. Silva, F.M. Sousa, M. Teixeira, P.N. Refojo, M.M. Pereira, Exploring membrane respiratory chains, Biochim. Biophys.

A unique property of the genus Nelumbo is that it can generate heat, which it does by using the alternative oxidase pathway (AOX). This pathway involves a different, alternative exchange of electrons from the usual pathway that electrons follow when generating energy in mitochondria, known as the AOX, or alternative oxidase pathway. The typical pathway in plant mitochondria involves cytochrome complexes. The pathway used to generate heat in Nelumbo involves cyanide-resistant alternative oxidase, which is a different electron acceptor than the usual cytochrome complexes.

The function of the electron transport chain is to produce this gradient. In all living organisms, a series of redox reactions is used to produce a transmembrane electrochemical potential gradient, or a so-called proton motive force (pmf). Redox reactions are chemical reactions in which electrons are transferred from a donor molecule to an acceptor molecule. The underlying force driving these reactions is the Gibbs free energy of the reactants and products. The Gibbs free energy is the energy available (“free”) to do work.

Because the fluoride ion is such a strong hydrogen bond acceptor, its salts tend to be hydrated and of limited solubility in organic solvents. As a fluoride ion source, TBAF solves this problem, although the nature of the fluoride is uncertain because TBAF samples are almost always hydrated, resulting in the formation of bifluoride (HF2−) hydroxide (OH−) as well as fluoride. Many applications tolerate heterogeneous or ill-defined fluoride sources. As a fluoride source in organic solvents, TBAF is used to remove silyl ether protecting groups.

To supply additional dissociation sites, other researchers have physically blended functionalized MWCNTs into P3HT polymer to create a P3HT-MWCNT with fullerene C60 double- layered device. However, the power efficiency was still relatively low at 0.01% under 100 mW/cm2 white illumination. Weak exciton diffusion toward the donor–acceptor interface in the bilayer structure may have been the cause in addition to the fullerene C60 layer possibly experiencing poor electron transport. More recently, a polymer photovoltaic device from C60-modified SWCNTs and P3HT has been fabricated.

Recognition of the appropriate tRNA by the synthetases is not mediated solely by the anticodon, and the acceptor stem often plays a prominent role. Reaction: # amino acid + ATP → aminophosphate + ADP # aminophosphate + tRNA → amino-tRNA + PPi Certain organisms can have one or more aminophosphate-tRNA synthetases missing. This leads to charging of the tRNA by a chemically related amino acid, and by use of an enzyme or enzymes, the tRNA is modified to be correctly charged. For example, Helicobacter pylori has glutaminyl tRNA synthetase missing.

By studying purple sulfur bacteria and green sulfur bacteria he was the first scientist to demonstrate, in 1931, that photosynthesis is a light-dependent redox reaction in which hydrogen from an oxidizable compound reduces carbon dioxide to cellular materials. Expressed as: :2 H2A + CO2 -> 2A + CH2O + H2O where A is the electron acceptor. His discovery predicted that H2O is the hydrogen donor in green plant photosynthesis and is oxidized to O2. The chemical summation of photosynthesis was a milestone in the understanding of the chemistry of photosynthesis.

AMDD otherwise known as Antimicrobial Drug Database is a biological database that seeks to consolidate antibacterial and antifungal drug information from a variety of sources such as PubChem, PubChem Bioassay, ZINC, ChemDB and DrugBank in order to advance the field of treatment of resistance microbes. As of 2012, AMDD contains ~2900 antibacterial and ~1200 antifungal compounds. These compounds are organized via their description, target, format, bioassay, molecular weight, hydrogen bond donor, hydrogen bond acceptor and rotatable bond. AMDD was built on Apache server 2.2.11.

Figure 2. Proposed methods of exoelectrogen electron transport: Direct Transfer, Transfer through Electron Shuttle, Transfer through Conductive Biofilm, Transfer through Conductive Pili. Reduced oxidoreductase enzymes at the extracellular membrane have been shown to use the following methods in transferring their electrons to the exogenous final acceptor: direct contact, shuttling via excreted mediators, iron chelating agents, through a conductive biofilm, and through conductive pili (Figure 2). However, the possibility exists that these methods are not mutually exclusive, and the method used may depend on environmental conditions.

Several are known to utilize promoters at map regions 4 and 38 to create variable transcripts along with polyadenylation signals at the right end of the genome. Small introns exist between map positions 444 and 46, and large introns exist between map positions 10 and 39. All messengers in MVM have small introns spliced while alternative splice donors and acceptor sites can also be used. During genome replication, read-through of the internal poly S site occurs and the large transcript is translated into a capsid protein.

Gene conversion is of two types - interallelic and interlocus gene conversions. The resurrection of seminal RNase gene function is believed to be the unexpected consequence of the interlocus gene conversion event of seminal RNase pseudogene with its homologous functional gene. In these recombination events, the genetic information is transferred from a donor functional locus to that of an acceptor pseudogene which is non- functional. Thus the non-functional seminal RNase pseudogene has acquired some new physiological functions being in the state of dead for many million years.

The alkali metals form complete series of compounds with all usually encountered anions, which well illustrate group trends. These compounds can be described as involving the alkali metals losing electrons to acceptor species and forming monopositive ions. This description is most accurate for alkali halides and becomes less and less accurate as cationic and anionic charge increase, and as the anion becomes larger and more polarisable. For instance, ionic bonding gives way to metallic bonding along the series NaCl, Na2O, Na2S, Na3P, Na3As, Na3Sb, Na3Bi, Na.

The manganese site forms a trigonal bipyramidal geometry with four ligands from the protein and a fifth solvent ligand. This solvent ligand is a hydroxide believed to serve as the electron acceptor of the enzyme. The active site cavity consists of a network of side chains of several residues associated by hydrogen bonding, extending from the aqueous ligand of the metal. Of note, the highly conserved residue Tyr34 plays a key role in the hydrogen-bonding network, as nitration of this residue inhibits the protein's catalytic ability.

In enzymology, a biochanin-A reductase () is an enzyme that catalyzes the chemical reaction :dihydrobiochanin A + NADP+ \rightleftharpoons biochanin A + NADPH + H+ Thus, the two substrates of this enzyme are dihydrobiochanin A and NADP+, whereas its 3 products are biochanin A, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is dihydrobiochanin-A:NADP+ Delta2-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.

In enzymology, an alpha-santonin 1,2-reductase () is an enzyme that catalyzes the chemical reaction :1,2-dihydrosantonin + NAD(P)+ \rightleftharpoons alpha- santonin + NAD(P)H + H+ The 3 substrates of this enzyme are 1,2-dihydrosantonin, NAD+, and NADP+, whereas its 4 products are alpha- santonin, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase.

A layer of copper phthalocyanine (CuPc) as electron donor and perylene tetracarboxylic derivative as electron acceptor, fabricating a cell with a fill factor as high as 0.65 and a power conversion efficiency of 1% under simulated AM2 illumination. Halls et al. fabricated a cell with a layer of bis(phenethylimido) perylene over a layer of PPV as the electron donor. This cell had peak external quantum efficiency of 6% and power conversion efficiency of 1% under monochromatic illumination, and a fill factor of up to 0.6.

The first is a smaller classifier, identifying donor splice sites and acceptor splice sites as well as start and stop codons. The second element involves constructing a full model using machine learning. Breaking the problem into two means that smaller targeted data sets can be used to train the classifiers, and that classifier can operate independently and be trained with smaller windows. The full model can use the independent classifier, and not have to waste computational time or model complexity re-classifying intron-exon boundaries.

Sendai virus Y proteins are initiated by ribosome shunting. Among 8 primary translation products of Sendai virus P/C mRNA, leaky scanning accounts for translation of protein C’, P, and C proteins, while expression of protein Y1 and Y2 is initiated via a ribosomal shunt discontinuous scanning. Scanning complex enters 5’ cap and scan ~50 nt of 5’ UTR, and then is transferred to an acceptor site at or close the Y initiation codons. In the case of Sendai virus, no specific donor site sequences are required.

This acid–base theory was a revival of oxygen theory of acids and bases, proposed by German chemist Hermann Lux in 1939, further improved by Håkon Flood circa 1947 and is still used in modern geochemistry and electrochemistry of molten salts. This definition describes an acid as an oxide ion () acceptor and a base as an oxide ion donor. For example: : + → : + → : + → + 2 This theory is also useful in the systematisation of the reactions of noble gas compounds, especially the xenon oxides, fluorides, and oxofluorides.

Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B Glycosyltransferases (GTFs, Gtfs) are enzymes (EC 2.4) that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based. The result of glycosyl transfer can be a carbohydrate, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyse transfer to inorganic phosphate or water.

In enzymology, a columbamine oxidase () is an enzyme that catalyzes the chemical reaction :2 columbamine + O2 \rightleftharpoons 2 berberine + 2 H2O Thus, the two substrates of this enzyme are columbamine and O2, whereas its two products are berberine and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is columbamine:oxygen oxidoreductase (cyclizing). This enzyme is also called berberine synthase.

Azobenzene reductase also known as azoreductase () is an enzyme that catalyzes the chemical reaction: :N,N-dimethyl-1,4-phenylenediamine + aniline + NADP+ \rightleftharpoons 4-(dimethylamino)azobenzene + NADPH + H+ The 3 substrates of this enzyme are N,N-dimethyl-1,4-phenylenediamine, aniline, and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are 4-(dimethylamino)azobenzene, nicotinamide adenine dinucleotide phosphate, and hydrogen ion. This enzyme belongs to the family of oxidoreductases, specifically those acting on other nitrogenous compounds as donors with NAD+ or NADP+ as acceptor.

In enzymology, a dimethylglycine oxidase () is an enzyme that catalyzes the chemical reaction :N,N-dimethylglycine + H2O + O2 \rightleftharpoons sarcosine + formaldehyde + H2O2 The 3 substrates of this enzyme are N,N-dimethylglycine, H2O, and O2, whereas its 3 products are sarcosine, formaldehyde, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N,N-dimethylglycine:oxygen oxidoreductase (demethylating). It employs one cofactor, FAD.

In enzymology, an oxalate oxidase () is an enzyme that catalyzes the chemical reaction :oxalate + O2 \+ 2 H+ \rightleftharpoons 2 CO2 \+ H2O2 The 3 substrates of this enzyme are oxalate, O2, and H+, whereas its two products are CO2 and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is oxalate:oxygen oxidoreductase. Other names in common use include aero-oxalo dehydrogenase, and oxalic acid oxidase.

In enzymology, a pyridoxine 4-oxidase () is an enzyme that catalyzes the chemical reaction :pyridoxine + O2 \rightleftharpoons pyridoxal + H2O2 Thus, the two substrates of this enzyme are pyridoxine and O2, whereas its two products are pyridoxal and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyridoxine:oxygen 4-oxidoreductase. Other names in common use include pyridoxin 4-oxidase, and pyridoxol 4-oxidase.

In enzymology, a phenylacetaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :phenylacetaldehyde + NAD+ \+ H2O \rightleftharpoons phenylacetate + NADH + 2 H+ The 3 substrates of this enzyme are phenylacetaldehyde, NAD+, and H2O, whereas its 3 products are phenylacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phenylacetaldehyde:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism and styrene degradation.

In enzymology, a pyruvate oxidase (CoA-acetylating) () is an enzyme that catalyzes the chemical reaction :pyruvate + CoA + O2 \rightleftharpoons acetyl-CoA + CO2 \+ H2O2 The 3 substrates of this enzyme are pyruvate, CoA, and O2, whereas its 3 products are acetyl-CoA, CO2, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (CoA-acetylating). This enzyme participates in pyruvate metabolism.

The efficiency of this energy transfer is inversely proportional to the sixth power of the distance between donor and acceptor, making FRET extremely sensitive to small changes in distance. Measurements of FRET efficiency can be used to determine if two fluorophores are within a certain distance of each other. Such measurements are used as a research tool in fields including biology and chemistry. FRET is analogous to near-field communication, in that the radius of interaction is much smaller than the wavelength of light emitted.

The inverse sixth-power distance dependence of Förster resonance energy transfer was experimentally confirmed by Wilchek, Edelhoch and Brand using tryptophyl peptides. Stryer, Haugland and Yguerabide also experimentally demonstrated the theoretical dependence of Förster resonance energy transfer on the overlap integral by using a fused indolosteroid as a donor and a ketone as an acceptor. However, a lot of contradictions of special experiments with the theory was observed. The reason is that the theory has approximate character and gives overestimated distances of 50–100 ångströms.

In enzymology, a formate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction :formate + NADP+ \rightleftharpoons CO2 \+ NADPH Thus, the two substrates of this enzyme are formate and NADP+, whereas its two products are CO2 and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is formate:NADP+ oxidoreductase. Other names in common use include NADP+-dependent formate dehydrogenase, and formate dehydrogenase (NADP+).

In enzymology, a hexose oxidase () is an enzyme that catalyzes the chemical reaction :D-glucose + O2 \rightleftharpoons D-glucono-1,5-lactone + H2O2 Thus, the two substrates of this enzyme are D-glucose and O2, whereas its two products are D-glucono-1,5-lactone and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D-hexose:oxygen 1-oxidoreductase. This enzyme participates in pentose phosphate pathway.

In enzymology, a 4-hydroxyphenylpyruvate oxidase () is an enzyme that catalyzes the chemical reaction :4-hydroxyphenylpyruvate + 1/2 O2 \rightleftharpoons 4-hydroxyphenylacetate + CO2 Thus, the two substrates of this enzyme are 4-hydroxyphenylpyruvate and O2, whereas its two products are 4-hydroxyphenylacetate and CO2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating). This enzyme participates in tyrosine metabolism.

In enzymology, a 6-oxohexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :6-oxohexanoate + NADP+ \+ H2O \rightleftharpoons adipate + NADPH + 2 H+ The 3 substrates of this enzyme are 6-oxohexanoate, NADP+, and H2O, whereas its 3 products are adipate, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-oxohexanoate:NADP+ oxidoreductase. This enzyme participates in caprolactam degradation.

In enzymology, a coniferyl-aldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :coniferyl aldehyde + H2O + NAD(P)+ \rightleftharpoons ferulate + NAD(P)H + 2 H+ The 4 substrates of this enzyme are coniferyl aldehyde, H2O, NAD+, and NADP+, whereas its 4 products are ferulate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase.

In enzymology, a formate dehydrogenase (cytochrome-c-553) () is an enzyme that catalyzes the chemical reaction :formate + ferricytochrome c-553 \rightleftharpoons CO2 \+ ferrocytochrome c-553 Thus, the two substrates of this enzyme are formate and ferricytochrome c-553, whereas its two products are CO2 and ferrocytochrome c-553. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase.

In enzymology, an ecdysone oxidase () is an enzyme that catalyzes the chemical reaction :ecdysone + O2 \rightleftharpoons 3-dehydroecdysone + H2O2 Thus, the two substrates of this enzyme are ecdysone and O2, whereas its two products are 3-dehydroecdysone and H2O2. This enzyme may or may not belong to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is ecdysone:oxygen 3-oxidoreductase. This enzyme might also called beta-ecdysone oxidase.

In enzymology, a hydrogen dehydrogenase () is an enzyme that catalyzes the chemical reaction :H2 \+ NAD+ \rightleftharpoons H+ \+ NADH Thus, the two substrates of this enzyme are H2 and NAD+, whereas its two products are H+ and NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydrogen:NAD+ oxidoreductase. Other names in common use include H2:NAD+ oxidoreductase, NAD+-linked hydrogenase, bidirectional hydrogenase, and hydrogenase.

In enzymology, a phosphonate dehydrogenase () is an enzyme that catalyzes the chemical reaction :phosphonate + NAD+ \+ H2O \rightleftharpoons phosphate + NADH + H+ The 3 substrates of this enzyme are phosphonate, NAD+, and H2O, whereas its 3 products are phosphate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on phosphorus or arsenic in donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is phosphonate:NAD+ oxidoreductase. Other names in common use include NAD:phosphite oxidoreductase, and phosphite dehydrogenase.

In enzymology, a putrescine oxidase () is an enzyme that catalyzes the chemical reaction :putrescine + O2 \+ H2O \rightleftharpoons 4-aminobutanal + NH3 \+ H2O2 The 3 substrates of this enzyme are putrescine, O2, and H2O, whereas its 3 products are 4-aminobutanal, NH3, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine:oxygen oxidoreductase (deaminating). This enzyme participates in urea cycle and metabolism of amino groups.

In enzymology, a lysine dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-lysine + NAD+ \rightleftharpoons 1,2-didehydropiperidine-2-carboxylate + NH3 \+ NADH + H+ Thus, the two substrates of this enzyme are L-lysine and NAD+, whereas its 4 products are 1,2-didehydropiperidine-2-carboxylate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-lysine:NAD+ oxidoreductase (deaminating, cyclizing).

The Cl/H exchange can then be undergone via reaction with K[HB(s-Bu)3] to give the germylene hydride cation in 91% yield. Synthesis of first stable monomeric germanium(II) hydride cation (a germyliumylidene hydride) The germylene hydride cation was also further reacted with the trityl cation, [Ph3C]+[B(C6F5)4]−, as a hydride scavenger, which resulted in the formation of an adduct with the three-coordinate germylene hydride cation acting a donor and a two-coordinate Ge(II) dication as an electron acceptor.

In enzymology, a leghemoglobin reductase () is an enzyme that catalyzes the chemical reaction :NAD(P)H + H+ \+ 2 ferrileghemoglobin \rightleftharpoons NAD(P)+ + 2 ferroleghemoglobin The 4 substrates of this enzyme are NADH, NADPH, H+, and ferrileghemoglobin, whereas its 3 products are NAD+, NADP+, and ferroleghemoglobin. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NAD(P)H:ferrileghemoglobin oxidoreductase. This enzyme is also called ferric leghemoglobin reductase.

In enzymology, a vomilenine reductase () is an enzyme that catalyzes the chemical reaction :1,2-dihydrovomilenine + NADP+ \rightleftharpoons vomilenine + NADPH + H+ Thus, the two substrates of this enzyme are 1,2-dihydrovomilenine and NADP+, whereas its 3 products are vomilenine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrovomilenine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

Förster coupling is the resonant energy transfer between excitons within adjacent QD's (quantum dots). The first studies of Forster were performed in the context of the sensitized luminescence of solids. Here, an excited sensitizer atom can transfer its excitation to a neighbouring acceptor atom, via an intermediate virtual photon. This same mechanism has also been shown to be responsible for exciton transfer between QD’s and within molecular systems and biosystems (though incoherently, as a mechanism for photosynthesis), all of which may be treated in a similar formulation.

Kochi's research examined the interactions of electron donors and acceptors. One topic of his study was the nitration of benzene to give nitrobenzene. Kochi's work showed that this reaction proceeds via a complex between benzene (the donor) and nitrosonium ion (the acceptor). He also contributed to many aspects of organometallic chemistry, including the discovery of Cu, Fe, and Ag-catalyzed cross-coupling processes (which preceded the discovery of the better known Pd and Ni- catalyzed versions), as well as several metal-catalyzed oxidative processes.

Most CB1 antagonists reported so far are close analogs or isosteres of rimonabant. A general CB1 inverse agonist pharmacophore model can be extracted from the common features of these analogs, diarylpyrazoles (Figure 4). This pharmacophore contains a cyclic core, C, (e.g. pyrazole in rimonabant) substituted by two aromatic moieties, A and B. A hydrogen bond acceptor unit, D, connects C with a cyclic lipophilic part, E. In some cases unit E directly connects to C. In Figure 4 rimonabant is used as an example.

Over 90% of methane is oxidized by microbes before it reaches the surface; this activity is "one of the most important controls on greenhouse gas emissions and climate on Earth." Reduced sulfur compounds such as elemental sulfur, hydrogen sulfide (H2S) and pyrite (FeS2) are found in hydrothermal vents in basaltic crust, where they precipitate out when metal- rich fluids contact seawater. Reduced iron compounds in sediments are mainly deposited or produced by anaerobic reduction of iron oxides. The electron acceptor with the highest redox potential is oxygen.

They are also well-established for third-period or heavier elements of groups 14–18 in their higher oxidation states. Ate complexes are a counterpart to onium ions. Lewis acids form ate ions when the central atom reacts with a donor (2 e– X-type ligand), gaining one more bond and becoming a negative-charged anion. Lewis bases form onium ions when the central atom reacts with an acceptor (0 e– Z-type ligand), gaining one more bond and becoming a positive-charged cation.

Just as there are a number of different electron donors (organic matter in organotrophs, inorganic matter in lithotrophs), there are a number of different electron acceptors, both organic and inorganic. In aerobic bacteria and facultative anaerobes if oxygen is available, it is invariably used as the terminal electron acceptor, because it generates the greatest Gibbs free energy change and produces the most energy. In anaerobic environments, different electron acceptors are used, including nitrate, nitrite, ferric iron, sulfate, carbon dioxide, and small organic molecules such as fumarate.

The most effective inhibitors have a hydrogen-bond acceptor at a specific distance away from a hydrophobic region. Inhibitors of oxidosqualene cyclase have shown promise as antimicrobial agents as well, because they’ve been shown to kill off trypanosoma cruzi. Trypanosoma cruzi is a parasite transmitted to people by insects, mostly in Latin America. The parasite causes a disease called Chagas disease, in which acute infections around an insect bite can lead to more serious complications, such as decreased heart, esophagus, colon, and even brain function.

These domains are joined by residue loops to form a substrate binding cleft, where the glucosyl group acceptor binds. Although H. orenii is a non-photosynthetic bacterium, various studies indicate that the structure of its SPS is similar to plant SPS. First, antibodies with high specificities for plant SPS also target the bacterial SPS, indicating the structure is conserved enough for the antibody to recognize the enzyme as an antigen. Furthermore, genomic studies reveal that closely related plant homologues exhibit up to 54% sequence identities.

In enzymology, a coniferyl-alcohol dehydrogenase () is an enzyme that catalyzes the chemical reaction :coniferyl alcohol + NADP+ \rightleftharpoons coniferyl aldehyde + NADPH + H+ Thus, the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD.

In enzymology, a L-idonate 5-dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-idonate + NAD(P)+ \rightleftharpoons 5-dehydrogluconate + NAD(P)H + H+ The 3 substrates of this enzyme are L-idonate, NAD+, and NADP+, whereas its 4 products are 5-dehydrogluconate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-idonate:NAD(P)+ oxidoreductase.

In enzymology, an indanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :indan-1-ol + NAD(P)+ \rightleftharpoons indanone + NAD(P)H + H+ The 3 substrates of this enzyme are indan-1-ol, NAD+, and NADP+, whereas its 4 products are indanone, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is indan-1-ol:NAD(P)+ 1-oxidoreductase.

In enzymology, an ephedrine dehydrogenase () is an enzyme that catalyzes the chemical reaction :(-)-ephedrine + NAD+ \rightleftharpoons (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+ Thus, the two substrates of this enzyme are (-)-ephedrine and NAD+, whereas its 3 products are (R)-2-methylimino-1-phenylpropan-1-ol, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (-)-ephedrine:NAD+ 2-oxidoreductase.

In enzymology, a vellosimine dehydrogenase () is an enzyme that catalyzes the chemical reaction :10-deoxysarpagine + NADP+ \rightleftharpoons vellosimine + NADPH + H+ Thus, the two substrates of this enzyme are 10-deoxysarpagine and NADP+, whereas its 3 products are vellosimine, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH- OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-deoxysarpagine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.

In enzymology, a salicylaldehyde dehydrogenase () is an enzyme that catalyzes the chemical reaction :salicylaldehyde + NAD+ \+ H2O \rightleftharpoons salicylate + NADH + 2 H+ The 3 substrates of this enzyme are salicylaldehyde, NAD+, and H2O, whereas its 3 products are salicylate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is salicylaldehyde:NAD+ oxidoreductase. This enzyme participates in naphthalene and anthracene degradation.

In enzymology, a triokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-glyceraldehyde \rightleftharpoons ADP + D-glyceraldehyde 3-phosphate Thus, the two substrates of this enzyme are ATP and D-glyceraldehyde, whereas its two products are ADP and D-glyceraldehyde 3-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glyceraldehyde 3-phosphotransferase. This enzyme is also called triose kinase.

In enzymology, an UMP kinase () is an enzyme that catalyzes the chemical reaction :ATP + UMP \rightleftharpoons ADP + UDP Thus, the two substrates of this enzyme are ATP and UMP, whereas its two products are ADP and UDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:UMP phosphotransferase. Other names in common use include uridylate kinase, UMPK, uridine monophosphate kinase, PyrH, UMP-kinase, and SmbA.

In enzymology, a thiamine kinase () is an enzyme that catalyzes the chemical reaction :ATP + thiamine \rightleftharpoons ADP + thiamine phosphate Thus, the two substrates of this enzyme are ATP and thiamine, whereas its two products are ADP and thiamine phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:thiamine phosphotransferase. Other names in common use include thiamin kinase (phosphorylating), thiamin phosphokinase, ATP:thiamin phosphotransferase, and thiamin kinase.

In enzymology, an acetylglutamate kinase () is an enzyme that catalyzes the chemical reaction: :ATP + N-acetyl-L-glutamate \rightleftharpoons ADP + N-acetyl-L-glutamyl 5-phosphate Thus, the two substrates of this enzyme are ATP and N-acetyl-L-glutamate, whereas its two products are ADP and N-acetyl-L- glutamyl 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. This enzyme participates in urea cycle and metabolism of amino groups.

In enzymology, a L-xylulokinase () is an enzyme that catalyzes the chemical reaction :ATP + L-xylulose \rightleftharpoons ADP + L-xylulose 5-phosphate Thus, the two substrates of this enzyme are ATP and L-xylulose, whereas its two products are ADP and L-xylulose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-xylulose 5-phosphotransferase. This enzyme is also called L-xylulokinase (phosphorylating).

In enzymology, a polyphosphate-glucose phosphotransferase () is an enzyme that catalyzes the chemical reaction. :(phosphate)n + D-glucose \rightleftharpoons (phosphate)n-1 + D-glucose 6-phosphate Thus, the two substrates of this enzyme are (phosphate)n and D-glucose, whereas its two products are (phosphate)n-1 and D-glucose 6-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is polyphosphate:D-glucose 6-phosphotransferase.

In enzymology, a nucleoside-phosphate kinase () is an enzyme that catalyzes the chemical reaction :ATP + nucleoside phosphate \rightleftharpoons ADP + nucleoside diphosphate Thus, the two substrates of this enzyme are ATP and nucleoside monophosphate, whereas its two products are ADP and nucleoside diphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:nucleoside-phosphate phosphotransferase. This enzyme is also called NMP- kinase, or nucleoside-monophosphate kinase.

In enzymology, an uridine kinase () is an enzyme that catalyzes the chemical reaction :ATP + uridine \rightleftharpoons ADP + UMP Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase.

In enzymology, 3-hydroxybutyrate dehydrogenase () is an enzyme that catalyzes the chemical reaction: :(R)-3-hydroxybutanoate + NAD+ \rightleftharpoons acetoacetate + NADH + H+ Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the synthesis and degradation of ketone bodies and the metabolism of butyric acid.

In enzymology, a sorbose reductase () is an enzyme that catalyzes the chemical reaction :D-glucitol + NADP+ \rightleftharpoons L-sorbose + NADPH + H+ Thus, the two substrates of this enzyme are D-glucitol and NADP+, whereas its 3 products are L-sorbose, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-glucitol:NADP+ oxidoreductase. This enzyme is also called Sou1p.

In enzymology, a D-ribulokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-ribulose \rightleftharpoons ADP + D-ribulose 5-phosphate Thus, the two substrates of this enzyme are ATP and D-ribulose, whereas its two products are ADP and D-ribulose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribulose 5-phosphotransferase. This enzyme is also called D-ribulokinase (phosphorylating).

In enzymology, a diphosphate-glycerol phosphotransferase () is an enzyme that catalyzes the chemical reaction :diphosphate + glycerol \rightleftharpoons phosphate + glycerol 1-phosphate Thus, the two substrates of this enzyme are diphosphate and glycerol, whereas its two products are phosphate and glycerol 1-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:glycerol 1-phosphotransferase. Other names in common use include PPi-glycerol phosphotransferase, and pyrophosphate-glycerol phosphotransferase.

In enzymology, a diphosphate-purine nucleoside kinase () is an enzyme that catalyzes the chemical reaction :diphosphate + a purine nucleoside \rightleftharpoons phosphate + a purine mononucleotide Thus, the two substrates of this enzyme are diphosphate and purine nucleoside, whereas its two products are phosphate and purine mononucleotide. This enzyme belongs to the family of transferases, specifically those transferring phosphorus- containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:purine nucleoside phosphotransferase. This enzyme is also called pyrophosphate-purine nucleoside kinase.

In enzymology, a D-arabinokinase () is an enzyme that catalyzes the chemical reaction :ATP + D-arabinose \rightleftharpoons ADP + D-arabinose 5-phosphate Thus, the two substrates of this enzyme are ATP and D-arabinose, whereas its two products are ADP and D-arabinose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-arabinose 5-phosphotransferase. This enzyme is also called D-arabinokinase (phosphorylating).

In enzymology, an ADP-specific glucokinase () also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction :ADP + D-glucose \rightleftharpoons AMP + D-glucose 6-phosphate Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate. This enzyme belongs to the family of transferases, to be specific those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. In humans, the ADP- dependent glucokinase is encoded by the ADPGK gene.

In enzymology, an ADP—thymidine kinase () is an enzyme that catalyzes the chemical reaction :ADP + thymidine \rightleftharpoons AMP + thymidine 5'-phosphate Thus, the two substrates of this enzyme are ADP and thymidine, whereas its two products are AMP and thymidine 5'-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:thymidine 5'-phosphotransferase. Other names in common use include ADP:dThd phosphotransferase, and adenosine diphosphate-thymidine phosphotransferase.

In enzymology, an agmatine kinase () is an enzyme that catalyzes the chemical reaction :ATP + agmatine \rightleftharpoons ADP + N4-phosphoagmatine Thus, the two substrates of this enzyme are ATP and agmatine, whereas its two products are ADP and N4-phosphoagmatine. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:agmatine N4-phosphotransferase. Other names in common use include phosphagen phosphokinase, and ATP:agmatine 4-N-phosphotransferase.

In enzymology, an alkylglycerone kinase () is an enzyme that catalyzes the chemical reaction :ATP + O-alkylglycerone \rightleftharpoons ADP + O-alkylglycerone phosphate Thus, the two substrates of this enzyme are ATP and O-alkylglycerone, whereas its two products are ADP and O-alkylglycerone phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:O-alkylglycerone phosphotransferase. Other names in common use include alkyldihydroxyacetone kinase (phosphorylating), and alkyldihydroxyacetone kinase.

In enzymology, a ceramide kinase, also abbreviated as CERK, () is an enzyme that catalyzes the chemical reaction: :ATP + ceramide \rightleftharpoons ADP + ceramide 1-phosphate Thus, the two substrates of this enzyme are ATP and ceramide, whereas its two products are ADP and ceramide-1-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ceramide 1-phosphotransferase. This enzyme is also called acylsphingosine kinase.

In enzymology, a glycerone kinase () is an enzyme that catalyzes the chemical reaction :ATP + glycerone \rightleftharpoons ADP + glycerone phosphate Thus, the two substrates of this enzyme are ATP and glycerone, whereas its two products are ADP and glycerone phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:glycerone phosphotransferase. Other names in common use include dihydroxyacetone kinase, acetol kinase, and acetol kinase (phosphorylating).

In enzymology, a hygromycin-B kinase () is an enzyme that catalyzes the chemical reaction :ATP + hygromycin B \rightleftharpoons ADP + 7"-O-phosphohygromycin Thus, the two substrates of this enzyme are ATP and hygromycin B, whereas its two products are ADP and 7-O-phosphohygromycin. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:hygromycin-B 7"-O-phosphotransferase. This enzyme is also called hygromycin B phosphotransferase.

In enzymology, a 6-hydroxyhexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction :6-hydroxyhexanoate + NAD+ \rightleftharpoons 6-oxohexanoate + NADH + H+ Thus, the two substrates of this enzyme are 6-hydroxyhexanoate and NAD+, whereas its 3 products are 6-oxohexanoate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 6-hydroxyhexanoate:NAD+ oxidoreductase. This enzyme participates in caprolactam degradation.

In enzymology, a 8-oxocoformycin reductase () is an enzyme that catalyzes the chemical reaction :coformycin + NADP+ \rightleftharpoons 8-oxocoformycin + NADPH + H+ Thus, the two substrates of this enzyme are coformycin and NADP+, whereas its 3 products are 8-oxocoformycin, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coformycin:NADP+ 8-oxidoreductase. This enzyme is also called 8-ketodeoxycoformycin reductase.

In enzymology, a (+)-borneol dehydrogenase () is an enzyme that increases the rate of, or catalyzes, the chemical reaction :(+)-borneol + NAD \rightleftharpoons (+)-camphor + NADH + H Thus, the two substrates of this enzyme are (+)-borneol and NAD, whereas its 3 products are (+)-camphor, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-borneol:NAD oxidoreductase. This enzyme is also called bicyclic monoterpenol dehydrogenase.

In enzymology, a (+)-neomenthol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-neomenthol + NADP \rightleftharpoons (−)-menthone + NADPH + H Thus, the two substrates of this enzyme are (+)-neomenthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-neomenthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis.

In enzymology, a (+)-sabinol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-cis-sabinol + NAD \rightleftharpoons (+)-sabinone + NADH + H Thus, the two substrates of this enzyme are (+)-cis-sabinol and NAD, whereas its 3 products are (+)-sabinone, NADH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (+)-cis-sabinol:NAD oxidoreductase. This enzyme is also called (+)-cis- sabinol dehydrogenase.

In enzymology, a 5-methyldeoxycytidine-5'-phosphate kinase () is an enzyme that catalyzes the chemical reaction :ATP + 5-methyldeoxycytidine 5'-phosphate \rightleftharpoons ADP + 5-methyldeoxycytidine diphosphate Thus, the two substrates of this enzyme are ATP and 5-methyldeoxycytidine 5'-phosphate, whereas its two products are ADP and 5-methyldeoxycytidine diphosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase.

In enzymology, an ureidoglycolate dehydrogenase () is an enzyme that catalyzes the chemical reaction :(S)-ureidoglycolate + NAD(P)+ \rightleftharpoons oxalureate + NAD(P)H + H+ The 3 substrates of this enzyme are (S)-ureidoglycolate, NAD+, and NADP+, whereas its 4 products are oxalureate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine metabolism.

In enzymology, a methylglyoxal reductase (NADPH-dependent) () is an enzyme that catalyzes the chemical reaction :lactaldehyde + NADP+ \rightleftharpoons methylglyoxal + NADPH + H+ Thus, the two substrates of this enzyme are lactaldehyde and NADP+, whereas its 3 products are methylglyoxal, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is lactaldehyde:NADP+ oxidoreductase. Other names in common use include lactaldehyde dehydrogenase (NADP+), and Gre2.

In enzymology, an octanol dehydrogenase () is an enzyme that catalyzes the chemical reaction :1-octanol + NAD+ \rightleftharpoons 1-octanal + NADH + H+ Thus, the two substrates of this enzyme are 1-octanol and NAD+, whereas its 3 products are 1-octanal, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is octanol:NAD+ oxidoreductase. This enzyme is also called 1-octanol dehydrogenase.

Fermentation is a specific type of heterotrophic metabolism that uses organic carbon instead of oxygen as a terminal electron acceptor. This means that these organisms do not use an electron transport chain to oxidize NADH to and therefore must have an alternative method of using this reducing power and maintaining a supply of for the proper functioning of normal metabolic pathways (e.g. glycolysis). As oxygen is not required, fermentative organisms are anaerobic. Many organisms can use fermentation under anaerobic conditions and aerobic respiration when oxygen is present.

Hexafluoroisopropanol, commonly abbreviated HFIP, is the organic compound with the formula (CF3)2CHOH. This fluoroalcohol finds use as solvent and synthetic intermediate. It appears as a colorless, volatile liquid that is characterized by a strong, pungent odor. As a solvent hexafluoro-2-propanol is polar and exhibits strong hydrogen bonding properties enabling it to dissolve substances that serve as hydrogen-bond acceptors, such as amides and ethers. (CF3)2CHCOH is classified as a hard Lewis acid and its acceptor properties are discussed in the ECW model.

In enzymology, a xylulokinase () is an enzyme that catalyzes the chemical reaction : ATP + D-xylulose ADP + D-xylulose 5-phosphate Thus, the two substrates of this enzyme are ATP and D-xylulose, whereas its two products are ADP and D-xylulose 5-phosphate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-xylulose 5-phosphotransferase. Other names in common use include xylulokinase (phosphorylating), and D-xylulokinase.

In contrast to ubiquitin, SUMO is not used to tag proteins for degradation. Mature SUMO is produced when the last four amino acids of the C-terminus have been cleaved off to allow formation of an isopeptide bond between the C-terminal glycine residue of SUMO and an acceptor lysine on the target protein. SUMO family members often have dissimilar names; the SUMO homologue in yeast, for example, is called SMT3 (suppressor of mif two 3). Several pseudogenes have been reported for this gene.

The MOS capacitor structure is the heart of the MOSFET. Consider a MOS capacitor where the silicon base is of p-type. If a positive voltage is applied at the gate, holes which are at the surface of the p-type substrate will be repelled by the electric field generated by the voltage applied. At first, the holes will simply be repelled and what will remain on the surface will be immobile (negative) atoms of the acceptor type, which creates a depletion region on the surface.

The proton on the carbon to which the hydroxyl group used to be attached is then transferred to Tyr272 (serving as the hydrogen acceptor), coupled with the oxidation of the substrate. One electron goes to the radical ligand, the other electron goes to the copper(II) center, which is then reduced to copper(I) as a result. Meanwhile, Tyr272 radical is also reduced. The proton subtraction step is rate determining and stereospecific since only the pro-S hydrogen on the alcohol carbon is removed (supported by studies of its kinetic isotope effect).

Shapiro–Senapathy algorithm can identify the cryptic splice sites, in addition to the authentic splice sites. Cryptic sites can often be stronger than the authentic sites, with a higher S&S; score. However, due to the lack of an accompanying complementary donor or acceptor site, this cryptic site will not be active or used in a splicing reaction. When a neighboring real site is mutated to become weaker than the cryptic site, then the cryptic site may be used instead of the real site, resulting in a cryptic exon and an aberrant transcript.

Besides the codon CAG, only TAG, which is a stop codon, was found at the ends of introns. Surprisingly, all three stop codons (TGA, TAA and TAG) were found after one base (G) at the start of introns. These stop codons are shown in the consensus canonical donor splice junction as AG:GT(A/G)GGT, wherein the TAA and TGA are the stop codons, and the additional TAG is also present at this position. The canonical acceptor splice junction is shown as (C/T)AG:GT, in which TAG is the stop codon.

Carbonate and hydoxo complexes of uranium(VI) as a function of pH The uranyl ion behaves as a hard acceptor and forms weaker complexes with nitrogen-donor ligands than with fluoride and oxygen donor ligands, such as hydroxide, carbonate, nitrate, sulfate and carboxylate. There may be 4, 5 or 6 donor atoms in the equatorial plane. In uranyl nitrate, [UO2(NO3)2]·2H2O, for example, there are six donor atoms in the equatorial plane, four from bidentate nitrato ligands and two from water molecules. The structure is described as hexagonal bipyramidal.

While non-electrostatic forces are present, these components remain similar over a wide variety of arenes, making the electrostatic model a useful tool in predicting relative binding energies. The other "effects" contributing to binding are not well understood. Polarization, donor-acceptor and charge-transfer interactions have been implicated; however, energetic trends do not track well with the ability of arenes and cations to take advantage of these effects. For example, if induced dipole was a controlling effect, aliphatic compounds such as cyclohexane should be good cation–π partners (but are not).

In the Lewis theory, a base is an electron pair donor which can share a pair of electrons with an electron acceptor which is described as a Lewis acid. The Lewis theory is more general than the Brønsted model because the Lewis acid is not necessarily a proton, but can be another molecule (or ion) with a vacant low-lying orbital which can accept a pair of electrons. One notable example is boron trifluoride (BF3). Some other definitions of both bases and acids have been proposed in the past, but are not commonly used today.

A Lewis base or electron-pair donor is a molecule with a high-energy pair of electrons which can be shared with a low-energy vacant orbital in an acceptor molecule to form an adduct. In addition to H+, possible acceptors (Lewis acids) include neutral molecules such as BF3 and metal ions such as Ag+ or Fe3+. Adducts involving metal ions are usually described as coordination complexes. According to the original formulation of Lewis, when a neutral base forms a bond with a neutral acid, a condition of electric stress occurs.

Some Bacteria and Archaea can aerobically oxidize elemental sulfur to sulfuric acid. Acidithiobacillus ferrooxidans and Thiobacillus thioparus can oxidize sulfur to sulfite by means of an oxygenase enzyme, although it is thought that an oxidase could be used as well as an energy saving mechanism. For the anaerobic oxidation of elemental sulfur, it is thought that the Sox pathway plays an important role, although this is not yet completely understood. Thiobacillus denitrificans uses oxidized forms on nitrogen as terminal electron acceptor instead of oxygen, and A. ferrooxidans uses ferrous iron.

Screening tools for the development of new cancer therapies are in high demand worldwide and often require the determination of enzyme kinetics. The high sensitivity of lanthanide luminescence, particularly of time-resolved luminescence has revealed to be an ideal candidate for this purpose. There are several ways of conducting this analysis by the use of fluorogenic enzyme substrates, substrates bearing donor/acceptor groups allowing fluorescence resonance energy transfer (FRET) and immunoassays. For example, guanine nucleotide binding proteins consist of several subunits, one of which comprises those of the Ras subfamily.

Box 3 and box 4 can vary its content although in most human USP enzyme domains each contain a conserved Cys-X-X-Cys motif, which is commonly associated with a zinc-binding site. USP27X has a length of 438 aminoacids. The residues that play a critical role in the active site can be found in position 87, in which resides the nucleophilic residue, and position 380 in which the proton acceptor is located. The number of aminoacids in USPs catalytic domain can vary from 295 and 850 residues.