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fmnh 2 + nad(p)+ fmn + nad(p)h + h + The 3 substrates of this enzyme are FMNH2 , NAD + , and NADP + , whereas its 4 products are FMN , NADH , 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.
FMN reductase (NAD(P)H) (EC 1.5.1.39, FRG) is an enzyme with systematic name FMNH 2:NAD(P) + oxidoreductase. [1] This enzyme catalyses the following chemical reaction.
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NADPH first transfers a hydride equivalent to FAD, creating FADH −, and then NADP + dissociates from the enzyme. Reduced PHBH then reacts with molecular oxygen to form the flavin-C(4a)-hydroperoxide. The flavin hydroperoxide quickly hydroxylates pOHB, and then eliminates water to regenerate oxidized flavin. [23]
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B 2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. [1]
NADH + NADP + + H + outside => NAD + + NADPH + H + inside. This redox reaction is a transfer of hydride equivalents from NADH to NADP + coupled to a translocation of protons across a membrane. NADP + is reduced to NADPH by NADH, which is oxidized into NAD +. This reduction is tied to the inward translocation of protons across a membrane. [2]