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  2. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    The number of flavin-dependent protein encoded genes in the genome (the flavoproteome) is species dependent and can range from 0.1% - 3.5%, with humans having 90 flavoprotein encoded genes. [16] FAD is the more complex and abundant form of flavin and is reported to bind to 75% of the total flavoproteome [ 16 ] and 84% of human encoded ...

  3. Mitochondrial matrix - Wikipedia

    en.wikipedia.org/wiki/Mitochondrial_matrix

    The citric acid cycle produces NADH and FADH2 through oxidation that will be reduced in oxidative phosphorylation to produce ATP. [ 2 ] [ 3 ] The cytosolic, intermembrane space , compartment has a higher aqueous:protein content of around 3.8 μL/mg protein relative to that occurring in mitochondrial matrix where such levels typically are near 0 ...

  4. Beta oxidation - Wikipedia

    en.wikipedia.org/wiki/Beta_oxidation

    If the acyl CoA contains a cis-Δ 3 bond, then cis-Δ 3-Enoyl CoA isomerase will convert the bond to a trans-Δ 2 bond, which is a regular substrate. If the acyl CoA contains a cis-Δ 4 double bond, then its dehydrogenation yields a 2,4-dienoyl intermediate, which is not a substrate for enoyl CoA hydratase.

  5. Oxoglutarate dehydrogenase complex - Wikipedia

    en.wikipedia.org/wiki/Oxoglutarate_dehydrogenase...

    The oxoglutarate dehydrogenase complex has the same subunit structure and thus uses the same cofactors as the pyruvate dehydrogenase complex and the branched-chain alpha-keto acid dehydrogenase complex (TTP, CoA, lipoate, FAD and NAD). Only the E3 subunit is shared in common between the three enzymes. [1]

  6. Fatty acyl-CoA esters - Wikipedia

    en.wikipedia.org/wiki/Fatty_acyl-CoA_esters

    To participate in specific metabolic processes, fatty acids must first be activated by being joined in thioester linkage (R-CO-SCoA) to the -SH group of coenzyme A, where R is a fatty carbon chain. The thioester bond is a high energy bond. [1] The activation reaction normally occurs in the endoplasmic reticulum or the outer mitochondrial membrane.

  7. Electron transport chain - Wikipedia

    en.wikipedia.org/wiki/Electron_transport_chain

    An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.

  8. Hydrogen carrier - Wikipedia

    en.wikipedia.org/wiki/Hydrogen_carrier

    The main role of these is to transport hydrogen atom to electron transport chain which will change ADP to ATP by adding one phosphate during metabolic processes (e.g. photosynthesis and respiration). Hydrogen carrier participates in an oxidation-reduction reaction [2] by getting reduced due to the acceptance of a Hydrogen.

  9. Flavoprotein - Wikipedia

    en.wikipedia.org/wiki/Flavoprotein

    The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid [13] Phenylacrylic acid decarboxylase (EC 4.1.1.102), an enzyme which confers resistance to cinnamic acid in yeast [14] Phototropin and cryptochrome, light-sensing proteins [15]