FAD
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| FAD | |
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| CAS number | [] |
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| Properties | |
| Molecular formula | C27H33N9O15P2 |
| Molar mass | 785.55 |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox disclaimer and references |
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In biochemistry, flavin adenine dinucleotide (FAD) is the precursor molecule to FADH2. Upon bonding to two hydrogen atoms, FAD is then changed to FADH2 and is turned into an energy-carrying molecule. FAD accommodates two equivalents of Hydrogen; both the hydride and the proton ions. This is used by organisms to carry out energy requiring processes. FAD, and the more common NAD, are reduced in the citric acid cycle during aerobic respiration.
FAD is a coenzyme derived from riboflavin, or vitamin B2. Many oxidoreductases, called flavoenzymes or flavoproteins, require FAD as a prosthetic group which functions in electron transfers. FADH2 may donate electrons either one or two at a time. In the citric acid cycle, FAD is a cofactor for the enzyme succinate dehydrogenase that oxidizes succinate to fumarate.
In the Krebs cycle, FAD is reduced to FADH2. These reduction potentials are used in the electron transport chain to generate ATP in the mitochondria, regenerating FAD.
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