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Flavin adenine dinucleotide

In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.

Flavin groupFlavin groupFlavins (from Latin flavus, "yellow") refers generally to the class of organic compounds generally derived from isoalloxazine by varying the R group shown:Flavins have extensive reduction-oxidation chemistry, and are named for the characteristic yellow color they exhibit in certain oxidation states. Their importance derives from biology: flavins are ubiquitous cofactors for biochemical redox reactions, particularly the electron transport chain.Flavin mononucleotideFlavin mononucleotideFlavin mononucleotide (FMN), or riboflavin-5′-phosphate, sold under the brand name Epioxa, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors.Cofactor (biochemistry)Cofactor (biochemistry)A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.FlavoproteinFlavoproteinFlavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes. Flavoproteins have either FMN (flavin mononucleotide) or FAD (flavin adenine dinucleotide) as a prosthetic group or as a cofactor.RedoxRedoxRedox ( , , reduction–oxidation or oxidation–reduction) is a type of chemical reaction in which the oxidation states of the reactants change. Oxidation is the loss of electrons or an increase in the oxidation state. Reduction is the gain of electrons or a decrease in the oxidation state. The oxidation and reduction processes occur simultaneously in the chemical reaction. Redox reactions fall into two classes.ProteinProteinBiomolecule consisting of chains of amino acid residuesA representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acidresidues.Oxidation stateIn chemistry, the oxidation state, or oxidation number, is the hypothetical charge of an atom assuming all of its bonds to other atoms are fully ionic. It describes the degree of oxidation (loss of electrons) of an atom in a chemical compound. Conceptually, the oxidation state may be positive, negative or zero. In a binary compound like KCl, oxidation state of +1 for K implies it has donated an electron Cl, which will have an oxidation state of -1.Amine oxideAmine oxideIn chemistry, an amine oxide, also known as an amine N-oxide or simply N-oxide, is a chemical compound that has the chemical formulaR3N−O. It contains a nitrogen-oxygencoordinate covalent bond with three additional hydrogen and/or substituent-groups attached to nitrogen. Sometimes it is written as R3N→O or, alternatively, as R3N=O. In the strict sense, the term amine oxide applies only to oxides of tertiary amines.Pyruvate dehydrogenase complexPyruvate dehydrogenase complexPyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. Acetyl-CoA may then be used in the citric acid cycle to carry out cellular respiration, and this complex links the glycolysis metabolic pathway to the citric acid cycle. Pyruvate decarboxylation is also known as the "pyruvate dehydrogenase reaction" because it also involves the oxidation of pyruvate.MetabolismMetabolismSet of chemical reactions in organismsSimplified view of cellular metabolismMetabolism (, from Greek μεταβολή (metabolē) 'change') refers to the set of life-sustaining chemical reactions that occur within living organisms.BiochemistryBiochemistryStudy of chemical processes of living organismsBiochemistry, or biological chemistry (distinct from chemical biology), is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines.Oxoglutarate dehydrogenase complexOxoglutarate dehydrogenase complexThe oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is a mitochondrialmultienzyme complex, most commonly known for its role in the citric acid cycle. It belongs to the family.

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