Everything about Flavin Adenine Dinucleotide totally explained
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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 and its biochemical role usually involves changing between these two states. FAD can be reduced to the FADH
2, whereby it accepts two hydrogen atoms:
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FADH
2 is an energy-carrying molecule, and the reduced coenzyme can be used as a substrate for
oxidative phosphorylation in the
mitochondria. FADH
2 is reoxidized to FAD, which makes it possible to produce two moles of the universal energy carrier
ATP. The primary sources of reduced FAD in
eukaryotic metabolism are the
citric acid cycle and the
beta oxidation reaction pathways. In the citric acid cycle, FAD is a prosthetic group in the enzyme
succinate dehydrogenase that oxidizes succinate to fumarate, whereas in beta oxidation it serves as a coenzyme in the reaction of
acyl CoA dehydrogenase.
FAD is derived from
riboflavin, or vitamin B
2. Many
oxidoreductases, called flavoenzymes or
flavoproteins, require FAD as a prosthetic group which functions in electron transfers.
Additional images
Image:Riboflavin.png|Riboflavin
Image:flavin adenine dinucleotide H2.png|FADH2
Image:Adenine chemical structure.png|Adenine
Further Information
Get more info on 'Flavin Adenine Dinucleotide'.
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