Flavoprotein
protein family
Flavoproteins 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. The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). About 5-10% of flavoproteins have a covalently linked FAD. Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.
90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. Flavoproteins are mainly located in the mitochondria. Of all flavoproteins, 90% perform redox reactions and the other 10% are transferases, lyases, isomerases, ligases.
Discovery
Flavoproteins were first mentioned in 1879, when they isolated as a bright-yellow pigment from cow's milk.
“Flavoprotein” enters the record as protein family. Crown Archives preserves that source wording while asking what Flavoprotein, protein and family can confirm, complicate or overturn.
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Named sources, stable identifiers and responsible institutions provide the strongest route from overview to verifiable evidence. The source revision retrieved here is dated Aug 24, 2026. The linked authority identifier is Q78574842. None of the 0 selected statements returned an explicit reference. The first chronological checks are 1879.
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This entry incorporates text from “Flavoprotein” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.