Riboflavin

Riboflavin

    • The flavin monoucleotide (FMN) and flavin adenine dinucleotide (FAD) are the two-coenzyme forms of riboflavin.
    • FMN and FAD serve as prosthetic groups of oxidation-reduction enzymes known as flavoenzymes or flavoproteins.
    • They are usually tightly, but not covalently, bound to the protein.
    • Many flavoproteins contain one or more metals as additional cofactors and are known as the metalloflavoproteins.
    • In the catalytic cycle of flavoproteins the flavin moiety of the flavin nucleotides undergoes reversible reduction of the isoalloxazine ring to yield the reduced nucleotides FMNH2 and FADH2.
    • L-amino acid oxidase contains tightly bound FMN as the prosthetic group.
    • Succinate dehydrogenase and D-amino acid oxidase contain FAD as prosthetic group.



     

Last modified: Wednesday, 28 March 2012, 5:26 PM