When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Flavin mononucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_mononucleotide

    During the catalytic cycle, various oxidoreductases induce reversible interconversions between the oxidized (FMN), semiquinone (FMNH •), and reduced (FMNH 2) forms of the isoalloxazine core. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. In its role as ...

  3. 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.

  4. 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 .

  5. Flavin-containing monooxygenase - Wikipedia

    en.wikipedia.org/wiki/Flavin-containing_mono...

    [18] [19] An example is the oxidation of glutathione to glutathione disulfide, both of which form a redox buffering system in the cell between the endoplasmic reticulum and the cytoplasm. yFMO is localized in the cytoplasm in order to maintain the optimum redox buffer ratio necessary for proteins containing disulfide bonds to fold properly. [18]

  6. 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 ...

  7. 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 + .

  8. Dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Dehydrogenase

    Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...

  9. Monooxygenase - Wikipedia

    en.wikipedia.org/wiki/Monooxygenase

    [2] [3] One important subset of the monooxygenases, the cytochrome P450 omega hydroxylases, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the cell signaling molecules, 20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating leukotriene B4 ...