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In biological systems, FAD acts as an acceptor of H + and e − in its fully oxidized form, an acceptor or donor in the FADH form, and a donor in the reduced FADH 2 form. The diagram below summarizes the potential changes that it can undergo. Along with what is seen above, other reactive forms of FAD can be formed and consumed.
The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). [1] About 5-10% of flavoproteins have a covalently linked FAD. [ 2 ] Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.
The oxidized and reduced forms are in fast equilibrium with the semiquinone form, shifted against the formation of the radical: [2] Fl ox + Fl red H 2 ⇌ FlH • where Fl ox is the oxidized flavin, Fl red H 2 the reduced flavin (upon addition of two hydrogen atoms) and FlH • the semiquinone form (addition of one hydrogen atom).
FAD is a unique electron acceptor. Its fully reduced form is FADH 2 (known as the hydroquinone form), but FAD can also be partially oxidized as FADH by either reducing FAD or oxidizing FADH 2. [11] Dehydrogenases typically fully reduce FAD to FADH 2. The production of FADH is rare.
1 FADH 2 : 6 H + : 6/4 ATP = 1 FADH 2 : 1.5 ATP. ATP : NADH+H + coming from glycolysis ratio during the oxidative phosphorylation is 1.5, as for FADH 2, if hydrogen atoms (2H + +2e −) are transferred from cytosolic NADH+H + to mitochondrial FAD by the glycerol phosphate shuttle located in the inner mitochondrial membrane.
66945 Ensembl ENSG00000073578 ENSMUSG00000021577 UniProt P31040 Q8K2B3 RefSeq (mRNA) NM_001294332 NM_004168 NM_001330758 NM_023281 RefSeq (protein) NP_001281261 NP_001317687 NP_004159 NP_075770 Location (UCSC) Chr 5: 0.22 – 0.26 Mb Chr 13: 74.47 – 74.5 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Succinate dehydrogenase complex, subunit A, flavoprotein variant is a protein ...
Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function. The following reaction is the oxidation of the fatty acid by FAD to afford an α,β-unsaturated fatty acid thioester of coenzyme A:
In enzymology, a FMN adenylyltransferase (EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction. ATP + FMN diphosphate + FAD. Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD.