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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]
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. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase.
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 FMNH2 + NAD(P) + ⇌ {\displaystyle \rightleftharpoons } FMN + NAD(P)H + H +
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NAD + to NADH. FMN to FMNH 2. CoQ to CoQH 2.. Complex I is the first enzyme of the mitochondrial electron transport chain.There are three energy-transducing enzymes in the electron transport chain - NADH:ubiquinone oxidoreductase (complex I), Coenzyme Q – cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV). [1]
This image of a simple structural formula is ineligible for copyright and therefore in the public domain, because it consists entirely of information that is common property and contains no original authorship.
Glutamate synthase catalyzes the conversion of 2-oxoglutarate into L-glutamate with L-glutamine serving as the nitrogen source for the reaction. All glutamate syntheses are iron-sulfur flavoproteins containing an iron-sulfur cluster and FMN. The three classes of glutamate syntheses are categorized based on their sequences and biochemical ...