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The flavin group is capable of undergoing oxidation-reduction reactions, and can accept either one electron in a two-step process or two electrons at once. Reduction is made with the addition of hydrogen atoms to specific nitrogen atoms on the isoalloxazine ring system: Equilibrium between the oxidized (left) and totally reduced (right) forms ...
Flavoproteins have either FMN (flavin mononucleotide) or FAD (flavin adenine dinucleotide) as a prosthetic group or as a cofactor. The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). [1] About 5-10% of flavoproteins have a covalently linked FAD. [2]
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The number of flavin-dependent protein encoded genes in the genome (the flavoproteome) is species dependent and can range from 0.1% - 3.5%, with humans having 90 flavoprotein encoded genes. [16] FAD is the more complex and abundant form of flavin and is reported to bind to 75% of the total flavoproteome [16] and 84% of human encoded ...
The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. [1] These enzymes can oxidize a wide array of heteroatoms , particularly soft nucleophiles , such as amines , sulfides , and phosphites .
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Flavodoxins (Fld) are small, soluble electron-transfer proteins. [1] [2] Flavodoxins contains flavin mononucleotide as prosthetic group.The structure of flavodoxin is characterized by a five-stranded parallel beta sheet, surrounded by five alpha helices. [3]
Members of this family utilise flavin mononucleotide as a cofactor and are often found to be homodimers. [ 1 ] [ 2 ] Members of this family include oxygen-insensitive NAD(P)H nitroreductase (flavin mononucleotide-dependent nitroreductase) ( 6,7-dihydropteridine reductase ) ( EC 1.5.1.34 ) and NADH dehydrogenase ( EC 1.6.99.3 ).