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  2. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    FAD is an aromatic ring system, whereas FADH 2 is not. [12] This means that FADH 2 is significantly higher in energy, without the stabilization through resonance that the aromatic structure provides. FADH 2 is an energy-carrying molecule, because, once oxidized it regains aromaticity and releases the energy represented by this stabilization ...

  3. Acyl-CoA - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA

    Acetyl-CoA is then used in the citric acid cycle while FADH2 and NADH are sent to the electron transport chain. [8] These intermediates all end up providing energy for the body as they are ultimately converted to ATP. [8] Example of Beta Oxidation using Stearic Acid. Beta oxidation, as well as alpha-oxidation, also occurs in the peroxisome. [1]

  4. Flavin group - Wikipedia

    en.wikipedia.org/wiki/Flavin_group

    There are 18 key atoms in isoalloxazine that make up its characteristic three-ring structure. The R-group varies and differentiates various flavins. Riboflavin. Flavins (from Latin flavus, "yellow") refers generally to the class of organic compounds containing the tricyclic heterocycle isoalloxazine or its isomer alloxazine, and derivatives thereof.

  5. Beta oxidation - Wikipedia

    en.wikipedia.org/wiki/Beta_oxidation

    Acetyl-CoA enters the citric acid cycle, generating NADH and FADH 2, which are electron carriers used in the electron transport chain. It is named as such because the beta carbon of the fatty acid chain undergoes oxidation and is converted to a carbonyl group to start the cycle all over again.

  6. Coenzyme A - Wikipedia

    en.wikipedia.org/wiki/Coenzyme_A

    Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate , and around 4% of cellular enzymes use it (or a thioester ) as a substrate.

  7. Acyl-CoA dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase

    Structure of the medium-chain acyl-CoA dehydrogenase tetramer. FAD molecules are shown in yellow. The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure of all ACADs, and is the most commonly deficient enzyme within the class that leads to metabolic disorders in animals. [1]

  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. Table of standard reduction potentials for half-reactions ...

    en.wikipedia.org/wiki/Table_of_standard...

    "Oxidation-reduction potentials, absorbance bands and molar absorbance of compounds used in biochemical studies" (PDF). Fasman GD, Editor. 1: 122– 130. Alberty, Robert A. (1998). "Calculation of standard transformed formation properties of biochemical reactants and standard apparent reduction potentials of half reactions".