Search results
Results from the WOW.Com Content Network
The midpoint potential of the NAD + /NADH redox pair is −0.32 volts, which makes NADH a moderately strong reducing agent. [7] The reaction is easily reversible, when NADH reduces another molecule and is re-oxidized to NAD +. This means the coenzyme can continuously cycle between the NAD + and NADH forms without being consumed. [5]
Out of the cytoplasm it goes into the Krebs cycle with the acetyl CoA. It then mixes with CO 2 and makes 2 ATP, NADH, and FADH. From there the NADH and FADH go into the NADH reductase, which produces the enzyme. The NADH pulls the enzyme's electrons to send through the electron transport chain. The electron transport chain pulls H + ions ...
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source').
The systematic name of this enzyme class is ATP:NADH 2'-phosphotransferase. Other names in common use include reduced nicotinamide adenine dinucleotide kinase (phosphorylating) , DPNH kinase , reduced diphosphopyridine nucleotide kinase , and NADH kinase .
The fish poison rotenone, the barbiturate drug amytal, and the antibiotic piericidin A inhibit NADH and coenzyme Q. [108] Carbon monoxide, cyanide, hydrogen sulphide and azide effectively inhibit cytochrome oxidase. Carbon monoxide reacts with the reduced form of the cytochrome while cyanide and azide react with the oxidised form.
Thus, the two substrates of this enzyme are L-glutamate and NAD +, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADH, and H +. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH 2 group of donors with NAD + or NADP + as acceptor. This enzyme participates in glutamate metabolism and nitrogen ...
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.
In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction. NADH + H + + H 2 O 2 NAD + + 2 H 2 O. The presumed function of NADH peroxidase is to inactivate H 2 O 2 generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H 2 O 2 causes damage to essential cellular components.