Flavin adenine dinucleotide

Flavin adenine dinucleotide
Identifiers
CAS Number	146-14-5 ;
3D model (JSmol)	quinone form: Interactive image; semiquinone form: Interactive image; hydroquinone form: Interactive image; flavin-N(5)-oxide form: Interactive image;
Beilstein Reference	1208946
ChEBI	CHEBI:16238 ;
ChEMBL	ChEMBL1232653 ;
ChemSpider	559059;
DrugBank	DB03147 ;
ECHA InfoCard	100.005.149
EC Number	205-663-1;
Gmelin Reference	108834
IUPHAR/BPS	5184;
KEGG	C00016 ;
MeSH	Flavin-Adenine+Dinucleotide
PubChem CID	643975;
UNII	ZC44YTI8KK ;
CompTox Dashboard (EPA)	DTXSID4048307 ;
	InChI InChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1 [PubChem] Key: VWWQXMAJTJZDQX-UYBVJOGSSA-N [PubChem];
	SMILES quinone form: c12cc(C)c(C)cc1N=C3C(=O)NC(=O)N=C3N2C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)OP(=O)(O)OC[C@@H]4[C@@H](O)[C@@H](O)[C@@H](O4)n5cnc6c5ncnc6N; semiquinone form: c12cc(C)c(C)cc1N[C]3C(=O)NC(=O)N=C3N2C[C@H](O)[C@H](O)[C@H](O)COP(=O)([O-])OP(=O)([O-])OC[C@@H]4[C@@H](O)[C@@H](O)[C@@H](O4)n5cnc6c5ncnc6N; hydroquinone form: c12cc(C)c(C)cc1NC=3C(=O)NC(=O)NC=3N2C[C@H](O)[C@H](O)[C@H](O)COP(=O)([O-])OP(=O)([O-])OC[C@@H]4[C@@H](O)[C@@H](O)[C@@H](O4)n5cnc6c5ncnc6N; flavin-N(5)-oxide form: c12cc(C)c(C)cc1[N+]([O-])=C3C(=O)NC(=O)N=C3N2C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)OP(=O)(O)OC[C@@H]4[C@@H](O)[C@@H](O)[C@@H](O4)n5cnc6c5ncnc6N;
Properties
Chemical formula	C27H33N9O15P2
Molar mass	785.557 g·mol−1
Appearance	White, vitreous crystals
log P	-1.336
Acidity (pKa)	1.128
Basicity (pKb)	12.8689
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). verify (what is ?) Infobox references

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. Intermediate oxidation states also exist, including which are the flavin-N(5)-oxide and semiquinone states.^[1] 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 superoxidized form of the flavin cofactor, the flavin-N(5)-oxide.^[2]^[3]

^ Teufel, Robin; Agarwal, Vinayak; Moore, Bradley S. (2016-04-01). "Unusual flavoenzyme catalysis in marine bacteria". Current Opinion in Chemical Biology. 31: 31–39. doi:10.1016/j.cbpa.2016.01.001. ISSN 1879-0402. PMC 4870101. PMID 26803009.
^ Teufel, R; Miyanaga, A; Michaudel, Q; Stull, F; Louie, G; Noel, JP; Baran, PS; Palfey, B; Moore, BS (28 November 2013). "Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement". Nature. 503 (7477): 552–6. Bibcode:2013Natur.503..552T. doi:10.1038/nature12643. PMC 3844076. PMID 24162851.
^ Teufel, Robin; Stull, Frederick; Meehan, Michael J.; Michaudel, Quentin; Dorrestein, Pieter C.; Palfey, Bruce; Moore, Bradley S. (2015-07-01). "Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor". Journal of the American Chemical Society. 137 (25): 8078–8085. Bibcode:2015JAChS.137.8078T. doi:10.1021/jacs.5b03983. ISSN 1520-5126. PMC 4720136. PMID 26067765.

[1] Teufel, Robin; Agarwal, Vinayak; Moore, Bradley S. (2016-04-01). "Unusual flavoenzyme catalysis in marine bacteria". Current Opinion in Chemical Biology. 31: 31–39. doi:10.1016/j.cbpa.2016.01.001. ISSN 1879-0402. PMC 4870101. PMID 26803009.

[:0-2] Teufel, R; Miyanaga, A; Michaudel, Q; Stull, F; Louie, G; Noel, JP; Baran, PS; Palfey, B; Moore, BS (28 November 2013). "Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement". Nature. 503 (7477): 552–6. Bibcode:2013Natur.503..552T. doi:10.1038/nature12643. PMC 3844076. PMID 24162851.

[:1-3] Teufel, Robin; Stull, Frederick; Meehan, Michael J.; Michaudel, Quentin; Dorrestein, Pieter C.; Palfey, Bruce; Moore, Bradley S. (2015-07-01). "Biochemical Establishment and Characterization of EncM's Flavin-N5-oxide Cofactor". Journal of the American Chemical Society. 137 (25): 8078–8085. Bibcode:2015JAChS.137.8078T. doi:10.1021/jacs.5b03983. ISSN 1520-5126. PMC 4720136. PMID 26067765.

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