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In enzymology, a fumarate reductase (NADH) (EC 1.3.1.6) is an enzyme that catalyzes the chemical reaction succinate + NAD + ⇌ {\displaystyle \rightleftharpoons } fumarate + NADH + H + Thus, the two substrates of this enzyme are succinate and NAD + , whereas its three products are fumarate , NADH , and H + .
The effects of the NAD + /NADH ratio are complex, controlling the activity of several key enzymes, including glyceraldehyde 3-phosphate dehydrogenase and pyruvate dehydrogenase. In healthy mammalian tissues, estimates of the ratio of free NAD + to NADH in the cytoplasm typically lie around 700:1; the ratio is thus favorable for oxidative reactions.
NMNH (Dihydronicotinamide mononucleotide), also known as reduced nicotinamide mononucleotide. [1] Both NMNH and NMN increase NAD+ levels in the body. [1] NAD+ is a universal coenzyme that plays vital roles in nearly all living organisms functioning in various biological processes such as metabolism, cell signaling, gene regulation, and DNA repair.
[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. Fumarate + 2 H + + 2 e − → Succinate +0.03 [9] O 2 + 2H + + 2e − → H 2 O 2 +0.30
The glycerol-3-phosphate shuttle is a mechanism used in skeletal muscle and the brain [1] that regenerates NAD + from NADH, a by-product of glycolysis. NADH is a reducing equivalent that stores electrons generated in the cytoplasm during glycolysis. NADH must be transported into the mitochondria to enter the oxidative phosphorylation pathway.
The following pictures depict general forms of some of the actions that FAD can be involved in. Mechanisms 1 and 2 represent hydride gain, in which the molecule gains what amounts to be one hydride ion. Mechanisms 3 and 4 radical formation and hydride loss. Radical species contain unpaired electron atoms and are very chemically active.
Oxidation of cytoplasmic NADH by the cytosolic form of the enzyme creates glycerol-3-phosphate from dihydroxyacetone phosphate. Once the glycerol-3-phosphate has moved through the outer mitochondrial membrane it can then be oxidised by a separate isoform of glycerol-3-phosphate dehydrogenase that uses quinone as an oxidant and FAD as a co-factor.
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 ...