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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.
The enzyme acyl-CoA thioesterase takes of the acyl-CoA to form a free fatty acid and coenzyme A. [4] ... FAD is the hydrogen acceptor, yielding FADH2. [7] 2.
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.
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.
The following reaction is the oxidation of the fatty acid by FAD to afford an α,β-unsaturated fatty acid thioester of coenzyme A: ACADs can be categorized into three distinct groups based on their specificity for short-, medium-, or long-chain fatty acid acyl-CoA substrates.
This reaction takes place on the inner mitochondrial membrane, allowing FADH 2 to donate its electrons directly to coenzyme Q which is part of the electron transport chain which ultimately transfers electrons to molecular oxygen O 2, with the formation of water, and the release of energy eventually captured in the form of ATP.
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.
Glycerol-3-phosphate is converted back to dihydroxyacetone phosphate by an inner membrane-bound mitochondrial glycerol-3-phosphate dehydrogenase 2 (GPD2 or mGPD), this time reducing one molecule of enzyme-bound flavin adenine dinucleotide (FAD) to FADH 2. FADH 2 then reduces coenzyme Q (ubiquinone to ubiquinol) whose electrons enter into ...