flavin adenine dinucleotide
Summary
Flavin adenine dinucleotide (FAD) is a crucial coenzyme derived from riboflavin (vitamin B2) that serves as an electron acceptor in cellular respiration and metabolism. It alternates between oxidized (FAD) and reduced (FADH2) forms, playing essential roles in the citric acid cycle, electron transport chain, and fatty acid oxidation.
Detail
FAD is a prosthetic group composed of riboflavin (vitamin B2) linked to adenine dinucleotide through a ribitol phosphate chain. In cellular metabolism, FAD functions as an electron acceptor, becoming reduced to FADH2 when it accepts two electrons and two protons. This occurs primarily in the citric acid cycle (succinate → fumarate reaction via succinate dehydrogenase) and during β-oxidation of fatty acids (acyl-CoA dehydrogenase reactions). FADH2 then donates electrons to Complex II (succinate dehydrogenase) of the electron transport chain, ultimately producing approximately 1.5 ATP molecules per FADH2 (compared to 2.5 ATP from NADH). FAD is also essential for amino acid metabolism, particularly in reactions catalyzed by monoamine oxidase and D-amino acid oxidase. Riboflavin deficiency leads to decreased FAD synthesis, resulting in ariboflavinosis with symptoms including cheilosis, glossitis, seborrheic dermatitis, and corneal vascularization.
Sources
- Lippincott's Illustrated Reviews: Biochemistry
- Lehninger Principles of Biochemistry
- First Aid for the USMLE Step 1
- Robbins Basic Pathology
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