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FAD
Identifiers
CAS number	146-14-5 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl][(2R,3S,4S)-2,3,4-trihydroxy] Y
PubChem	703, 24868262 [(2R,3S,4R)-3,4-dihydroxy, -2-yl], 439154 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl], 25164505 [(3R,4R,5R)-5-purinyl, -3,4-dihydroxy][(2R,3R,4R)-2,3,4-trihydroxy], 5288191 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl][(2R,3S,4R)-2,3,4-trihydroxy], 643975 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl][(2R,3S,4S)-2,3,4-trihydroxy]
ChemSpider	683 N, 388300 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl] Y, 4450403 [(2R,3S,4R,5R)-5-purinyl, -3,4-dihydroxy, -2-yl][(2R,3S,4R)-2,3,4-trihydroxy] Y
UNII	ZC44YTI8KK Y
EC number	205-663-1
DrugBank	DB03147
KEGG	D00005 N
MeSH	Flavin-Adenine+Dinucleotide
ChEBI	CHEBI:16238 Y
ChEMBL	CHEMBL1232663 N
Beilstein Reference	1208946
Gmelin Reference	108834
3DMet	B04619
Jmol-3D images	Image 1
SMILES Cc1cc2nc3c(nc(O)nc3=O)n(CC(O)C(O)C(O)COP(O)(=O)OP(O)(=O)OCC3OC(C(O)C3O)n3cnc4c(N)ncnc34)c2cc1C
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) N Key: VWWQXMAJTJZDQX-UHFFFAOYSA-N N InChI=1/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) Key: VWWQXMAJTJZDQX-UYBVJOGSBL
Properties
Molecular formula	C27H33P2N9O15
Molar mass	785.5497 g mol-1
Appearance	White, vitreous crystals
log P	-1.336
Acidity (pKa)	1.128
Basicity (pKb)	12.8689
N (verify) (what is: Y/N?) Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

In biochemistry, flavin adenine dinucleotide (FAD) is a redox cofactor involved in several important reactions in metabolism. FAD can exist in two different redox states, which it converts between by accepting or donating electrons. The molecule consists of a riboflavin moiety (vitamin B₂) bound to the phosphate group of an ADP molecule. The flavin group is bound to ribitol, a sugar alcohol, by a carbon-nitrogen bond, not a glycosidic bond. Thus, riboflavin is not technically a nucleotide; the name flavin adenine dinucleotide is a misnomer.^[1]

FAD can be reduced to FADH₂, whereby it accepts two hydrogen atoms (a net gain of two electrons):

FAD (fully oxidized form, or quinone form) accepts two electrons and two protons to become FADH2 (hydroquinone form). FADH2 can then be oxidized to the semireduced form (semiquinone) FADH by donating one electron and one proton. The semiquinone is then oxidized once more by losing an electron and a proton and is returned to the initial quinone form (FAD).

FAD is an aromatic ring system, whereas FADH₂ is not. This means that FADH₂ is significantly higher in energy, without the stabilization that aromatic structure provides. FADH₂ is an energy-carrying molecule, because, if it is oxidized, it will regain aromaticity and release all the energy represented by this stabilization.

The primary biochemical role of FADH₂ in eukaryotes is to carry high-energy electrons used for oxidative phosphorylation. FAD is a prosthetic group in the enzyme complex succinate dehydrogenase (complex II) that oxidizes succinate to fumarate in the eighth step of the citric acid cycle. The high-energy electrons from this oxidation are stored momentarily by reducing FAD to FADH₂. FADH₂ then reverts to FAD, sending its two high-energy electrons through the electron transport chain; the energy in FADH₂ is enough to produce 1.5 equivalents of ATP^[2] by oxidative phosphorylation. Another metabolic source of FADH₂ is beta oxidation, where FAD serves as a coenzyme to acyl CoA dehydrogenase.

Any oxidoreductase enzyme that uses FAD as an electron carrier is called a flavoprotein. There are many flavoproteins besides components of the succinate dehydrogenase complex, including α-ketoglutarate dehydrogenase and a component of the pyruvate dehydrogenase complex.

Additional images [link]

• 

  Riboflavin

• 

  FADH2

• 

  Adenine

See also [link]

• Flavin mononucleotide
• NAD

External links [link]

• FAD bound to proteins in the PDB

References [link]