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  2. Flavin mononucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_mononucleotide

    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]

  3. P450-containing systems - Wikipedia

    en.wikipedia.org/wiki/P450-containing_systems

    These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome b 5 transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains.

  4. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    The two electrons on reduced FAD (FADH 2) are transferred one at a time to FMN and then a single electron is passed from FMN to the heme of the P450. [ 24 ] The P450 systems that are located in the mitochondria are dependent on two electron transfer proteins: An FAD containing adrenodoxin reductase (AR) and a small iron-sulfur group containing ...

  5. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    Oxidative phosphorylation in the eukaryotic mitochondrion is the best-understood example of this process. The mitochondrion is present in almost all eukaryotes, with the exception of anaerobic protozoa such as Trichomonas vaginalis that instead reduce protons to hydrogen in a remnant mitochondrion called a hydrogenosome .

  6. Flavin group - Wikipedia

    en.wikipedia.org/wiki/Flavin_group

    The flavin moiety is often attached with an adenosine diphosphate to form flavin adenine dinucleotide (FAD), and, in other circumstances, is found as flavin mononucleotide (or FMN), a phosphorylated form of riboflavin. It is in one or the other of these forms that flavin is present as a prosthetic group in flavoproteins.

  7. Flavoprotein - Wikipedia

    en.wikipedia.org/wiki/Flavoprotein

    90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. [4] Flavoproteins are mainly located in the mitochondria . [ 4 ] Of all flavoproteins, 90% perform redox reactions and the other 10% are transferases , lyases , isomerases , ligases .

  8. FMN reductase - Wikipedia

    en.wikipedia.org/wiki/FMN_reductase

    In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction FMNH 2 + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 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 + .

  9. FMN reductase (NADPH) - Wikipedia

    en.wikipedia.org/wiki/FMN_reductase_(NADPH)

    Download as PDF; Printable version; In other projects Wikidata item; Appearance. move to sidebar hide ... FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, ...