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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. 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 ...

  4. Flavin group - Wikipedia

    en.wikipedia.org/wiki/Flavin_group

    The flavin group is capable of undergoing oxidation-reduction reactions, and can accept either one electron in a two-step process or two electrons at once. Reduction is made with the addition of hydrogen atoms to specific nitrogen atoms on the isoalloxazine ring system: Equilibrium between the oxidized (left) and totally reduced (right) forms ...

  5. Template:List of oxidation states of the elements - Wikipedia

    en.wikipedia.org/wiki/Template:List_of_oxidation...

    The oxidation states are also maintained in articles of the elements (of course), and systematically in the table {{Infobox element/symbol-to-oxidation-state}} See also [ edit ]

  6. Cofactor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Cofactor_(biochemistry)

    The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).

  7. Template : List of oxidation states of the elements/sandbox

    en.wikipedia.org/wiki/Template:List_of_oxidation...

    The oxidation states are also maintained in articles of the elements (of course), and systematically in the table {{Infobox element/symbol-to-oxidation-state}} See also [ edit ]

  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. Periodic table - Wikipedia

    en.wikipedia.org/wiki/Periodic_table

    No element heavier than einsteinium (element 99) has ever been observed in macroscopic quantities in its pure form, nor has astatine; francium (element 87) has been only photographed in the form of light emitted from microscopic quantities (300,000 atoms). [14] Of the 94 natural elements, eighty have a stable isotope and one more has an almost ...