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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 ...
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). In the form of FADH 2, it is one of the cofactors that can transfer electrons to the electron transfer chain.
At the inner mitochondrial membrane, electrons from NADH and FADH 2 pass through the electron transport chain to oxygen, which provides the energy driving the process as it is reduced to water. [4] The electron transport chain comprises an enzymatic series of electron donors and acceptors.
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.
Oxaloacetate + 2 H + + 2 e − → Malate -0.17 [ 10 ] While under standard conditions malate cannot reduce the more electronegative NAD + :NADH couple, in the cell the concentration of oxaloacetate is kept low enough that Malate dehydrogenase can reduce NAD + to NADH during the citric acid cycle .
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 ...
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.
NADH and FADH 2 are produced in the matrix or transported in through porin and transport proteins in order to undergo oxidation through oxidative phosphorylation. [1] NADH and FADH 2 undergo oxidation in the electron transport chain by transferring an electrons to regenerate NAD + and FAD.