Flavin adenine dinucleotide

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(Redirected from FADH)

Flavin adenine dinucleotide (FAD) is a redox cofactor involved in several important metabolic reactions. It is a molecule that is synthesized from riboflavin (vitamin B2) and adenosine triphosphate (ATP).

Structure[edit | edit source]

FAD consists of two major portions: the adenine and flavin moieties. The adenine portion is composed of a nitrogenous base attached to a five-carbon sugar, ribose, which is further connected to a chain of three phosphate groups. The flavin portion is a ring structure known as isoalloxazine, which is attached to the ribityl part of the molecule.

Function[edit | edit source]

FAD is a crucial component in oxidation-reduction reactions. It acts as a hydrogen acceptor in dehydrogenation reactions, becoming reduced to FADH2. This reduced form can then donate these hydrogen atoms in subsequent reactions, returning to its oxidized state.

Role in Metabolic Pathways[edit | edit source]

FAD is involved in several metabolic pathways, including:

  • Krebs cycle: FAD is a key player in the Krebs cycle, where it is reduced to FADH2 in the succinate dehydrogenase reaction.
  • Beta oxidation: In the process of beta oxidation, FAD is reduced to FADH2 during the oxidation of fatty acids.
  • Electron transport chain: FADH2 donates its electrons to the electron transport chain, contributing to the production of ATP.

Deficiency[edit | edit source]

A deficiency in FAD can lead to a variety of health problems, including dermatitis, glossitis, and neurological symptoms. This is often due to a deficiency in dietary riboflavin, as the body cannot synthesize FAD without this vitamin.

See Also[edit | edit source]

Flavin adenine dinucleotide Resources
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Contributors: Prab R. Tumpati, MD