Search results
Results from the WOW.Com Content Network
FAD is converted between these states by accepting or donating electrons. FAD, in its fully oxidized form, or quinone form, accepts two electrons and two protons to become FADH 2 (hydroquinone form). The semiquinone (FADH ·) can be formed by either reduction of FAD or oxidation of FADH 2 by accepting or donating one electron and one proton ...
FADH and FADH 2 are reduced forms of FAD. FADH 2 is produced as a prosthetic group in succinate dehydrogenase, an enzyme involved in the citric acid cycle. In oxidative phosphorylation, two molecules of FADH 2 typically yield 1.5 ATP each, or three ATP combined.
FAD + 2 H + + 2 e − → FADH 2 (coenzyme bonded to flavoproteins) −0.22 Depending on the protein involved, the potential of the flavine can vary widely [8]
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. [3] 90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. [4]
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.
It uses FAD as an electron acceptor and it is reduced to FADH 2. Trans-delta 2-enoyl CoA is hydrated at the double bond to produce L-3-hydroxyacyl CoA by enoyl-CoA hydratase. L-3-hydroxyacyl CoA is dehydrogenated again to create 3-ketoacyl CoA by 3-hydroxyacyl CoA dehydrogenase. This enzyme uses NAD as an electron acceptor.
Mitochondrial glycerol-3-phosphate dehydrogenase (mGPD) then catalyzes the oxidation of G3P by FAD, regenerating DHAP in the cytosol and forming FADH 2 in the mitochondrial matrix. [4] In mammals, its activity in transporting reducing equivalents across the mitochondrial membrane is secondary to the malate–aspartate shuttle.
FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides. Mutation in ETFs can lead to deficiency of passing reducing equivalent of FADH 2 to electron transport chain, causing Glutaric acidemia type 2