flavin adenine dinucleotide
Also known as FAD, adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate], Riboflavin 5'-adenosine diphosphate, Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine, Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine, Adenine-flavine dinucleotide, Flavitan, Flavin adenine dinucleotide oxidized
redox cofactor, more specifically a prosthetic group, involved in several important reactions in metabolism; can exist in three (or four: flavin-N(5)-oxide) different redox states; converted between these states by accepting or donating electrons
Chemical data
- Formula
- C27H33N9O15P2
- Molecular weight
- 785.5 g/mol
- IUPAC name
- [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3S,4S)-5-(7,8-dimethyl-2,4-dioxobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] hydrogen phosphate
- SMILES
- CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)OP(=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=NC6=C(N=CN=C65)N)O)O)O)O)O
- InChIKey
- VWWQXMAJTJZDQX-UYBVJOGSSA-N
- XLogP
- -5
- Polar surface area
- 356 Ų
- H-bond donors
- 9
- H-bond acceptors
- 20
- Formal charge
- 0
via PubChem
Research
Article
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). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.
FAD exists in two common oxidation states, the fully oxidized form (FAD) and the fully reduced, dihydrogenated form, FADH2. Other oxidation states also exist, including the N-oxide and semiquinone states. FAD, in its fully oxidized form, accepts two electrons and two protons to become FADH2. The semiquinone (FADH) can be formed by either reduction of FAD or oxidation of FADH2 by accepting or donating one electron and one proton, respectively. Some proteins, however, generate and maintain a super oxidized form of the flavin cofactor, the flavin-N(5)-oxide.