Search results
Results from the WOW.Com Content Network
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN).
Hydrogen bonding of the substrate's carbonyl oxygen to both the 2'-OH of the ribityl side-chain of FAD and to the main chain N-H of the previously mentioned glutamate residue lowers the pKa of this proton, allowing it to be readily removed by glutamate. [1] Close-up of the medium-chain acyl-CoA dehydrogenase active site. FAD is bound.
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
Reaction catalyzed by an oxidase, note the reduction of oxygen as the electron acceptor. Dehydrogenase and oxidase are easily distinguishable if one considers the electron acceptor. An oxidase will remove electrons from a substrate as well, but only uses oxygen as its electron acceptor. One such reaction is: AH 2 + O 2 ↔ A + H 2 O 2.
Although cellular respiration is technically a combustion reaction, it is an unusual one because of the slow, controlled release of energy from the series of reactions. Nutrients that are commonly used by animal and plant cells in respiration include sugar , amino acids and fatty acids , and the most common oxidizing agent is molecular oxygen ...
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin.These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair.
This reaction proceeds in three steps: decarboxylation of α-ketoglutarate, reduction of NAD + to NADH, and subsequent transfer to CoA, which forms the end product, succinyl CoA. ΔG°' for this reaction is -7.2 kcal mol −1. The energy needed for this oxidation is conserved in the formation of a thioester bond of succinyl CoA.
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).