Flavin adenine dinucleotide

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"FAD" redirects here. For other uses, see FAD (disambiguation).
Flavin adenine dinucleotide
Stereo, Kekulé, skeletal formula of FAD
Spacefill model of FAD
Ball and stick model of FAD
Identifiers
CAS number 146-14-5 YesY
PubChem 643975
UNII ZC44YTI8KK YesY
EC number 205-663-1
DrugBank DB03147
KEGG D00005 N
MeSH Flavin-Adenine+Dinucleotide
ChEBI CHEBI:16238 YesY
ChEMBL CHEMBL1232653 N
Beilstein Reference 1208946
Gmelin Reference 108834
3DMet B04619
Jmol-3D images Image 1
Properties
Molecular formula C27H33N9O15P2
Molar mass 785.55 g mol−1
Appearance White, vitreous crystals
log P -1.336
Acidity (pKa) 1.128
Basicity (pKb) 12.8689
Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
 N (verify) (what is: YesY/N?)
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 FADH2 equlibrium.png

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. Its hydrogens remain in the mitochondrial matrix, whilst FAD is tightly bound to a dehydrogenase enzyme i.e. the second protein complex in the oxidative phosphorylation chain. 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.

A flavoprotein is a protein that contains a flavin moiety, this may be in the form of FAD or FMN (Flavin mononucleotide) . There are many flavoproteins besides components of the succinate dehydrogenase complex, including α-ketoglutarate dehydrogenase and a component of the pyruvate dehydrogenase complex.

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References[edit]

  1. ^ Metzler DE, (2001) Biochemistry. The chemical reactions of living cells, 2nd edition, Harcourt, San Diego
  2. ^ Stryer, (2006) Biochemistry