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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 + .
Glycolysis produces only 2 ATP molecules, but somewhere between 30 and 36 ATPs are produced by the oxidative phosphorylation of the 10 NADH and 2 succinate molecules made by converting one molecule of glucose to carbon dioxide and water, [6] while each cycle of beta oxidation of a fatty acid yields about 14 ATPs. These ATP yields are ...
Bacteria can use several different electron donors. When organic matter is the electron source, the donor may be NADH or succinate, in which case electrons enter the electron transport chain via NADH dehydrogenase (similar to Complex I in mitochondria) or succinate dehydrogenase (similar to Complex II).
Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration. [1] The catalyzed reaction is: succinate + acceptor <=> fumarate + reduced acceptor. Fumarate reductases can be divided into two classes depending on the electron acceptor: Fumarate reductase (NADH ...
The NADH generated in the citric acid cycle may later be oxidized (donate its electrons) to drive ATP synthesis in a type of process called oxidative phosphorylation. [6] FADH 2 is covalently attached to succinate dehydrogenase , an enzyme which functions both in the citric acid cycle and the mitochondrial electron transport chain in oxidative ...
Both NAD + and NADH strongly absorb ultraviolet light because of the adenine. For example, peak absorption of NAD + is at a wavelength of 259 nanometers (nm), with an extinction coefficient of 16,900 M −1 cm −1. NADH also absorbs at higher wavelengths, with a second peak in UV absorption at 339 nm with an extinction coefficient of 6,220 M ...
The latter is the case when the substrate is succinate or extramitochondrial NADH being oxidized via the glycerol phosphate shuttle; or other UQH2-linked dehydrogenase. During normal aerobic respiration the ratio would be somewhere between these values, as the TCA cycle produces both NADH and ubiquinol.
[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