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	<title>Translations:Flavin adenine dinucleotide/18/en - Revision history</title>
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	<updated>2026-07-11T04:19:22Z</updated>
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		<title>FuzzyBot: Importing a new version from external source</title>
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		<updated>2024-04-10T10:54:10Z</updated>

		<summary type="html">&lt;p&gt;Importing a new version from external source&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;FAD has a more positive [[reduction potential]] than [[NAD+]] and is a very strong oxidizing agent. The cell utilizes this in many energetically difficult oxidation reactions such as dehydrogenation of a C-C bond to an [[alkene]]. FAD-dependent proteins function in a large variety of metabolic pathways including electron transport, DNA repair, nucleotide biosynthesis, [[Beta oxidation|beta-oxidation]] of fatty acids, amino acid catabolism, as well as synthesis of other cofactors such as [[Coenzyme A|CoA]], [[CoQ]] and [[heme]] groups.  One well-known reaction is part of the [[citric acid cycle]] (also known as the TCA or Krebs cycle); [[succinate dehydrogenase]] (complex II in the [[electron transport chain]]) requires covalently bound FAD to catalyze the oxidation of [[succinate]] to [[fumarate]] by coupling it with the reduction of [[ubiquinone]] to [[ubiquinol]]. The high-energy electrons from this oxidation are stored momentarily by reducing FAD to FADH&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt;. FADH&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; then reverts to FAD, sending its two high-energy electrons through the electron transport chain; the energy in FADH&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; is enough to produce 1.5 equivalents of [[Adenosine triphosphate|ATP]] by [[oxidative phosphorylation]]. Some redox flavoproteins non-covalently bind to FAD like [[acyl CoA dehydrogenase|Acetyl-CoA-dehydrogenases]] which are involved in [[beta-oxidation]] of fatty acids and catabolism of amino acids like [[leucine]] ([[isovaleryl-CoA dehydrogenase]]), [[isoleucine]], (short/branched-chain acyl-CoA dehydrogenase), [[valine]] (isobutyryl-CoA dehydrogenase), and [[lysine]] ([[glutaryl-CoA dehydrogenase]]).  Additional examples of FAD-dependent enzymes that regulate metabolism are [[glycerol-3-phosphate dehydrogenase]] (triglyceride synthesis) and [[xanthine oxidase]] involved in [[purine]] nucleotide catabolism.  Noncatalytic functions that FAD can play in flavoproteins include as structural roles, or involved in blue-sensitive light [[photoreceptor cell|photoreceptors]] that regulate [[circadian clock|biological clocks]] and development, generation of light in [[bioluminescent]] bacteria.&lt;/div&gt;</summary>
		<author><name>FuzzyBot</name></author>
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