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Any of a number of conjugated protein dehydrogenases containing flavin that play a role in biological oxidations in both plants and animals; a yellow enzyme.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.



(also flavin enzyme or yellow enzyme), any one of a group of complex enzymes, whose riboflavin derivatives—flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN)—serve as prosthetic groups (non-protein components). Flavoproteins were discovered in 1932 by O. Warburg.

The prosthetic group of many flavoproteins contains, in addition to flavin nucleotides, metals (Fe, Cu, Mo), sulfur compounds, and other compounds. The metals are complexly bound to the flavin nucleotides. When in an oxidized state, most flavoproteins are colored yellow and have characteristic absorption bands in the ranges 350–380 and 450–460 nanometers; in a reduced state, they are colorless. Flavoproteins are related to the oxidoreductase class and catalyze important oxidation-reduction reactions in living organisms with the direct participation of FAD and, more rarely, FMN. The specificity (selectivity) and effectiveness of the action of flavoproteins are determined by the nature of their protein components (apoenzymes), which have still not been adequately studied. Most flavoproteins are associated with cell membranes, forming strong complexes with lipids that are part of their composition.

The primary function of flavoproteins is the oxidation of reduced nicotinamide adenine dinucleotide in electron transfer chains (seeOXIDATIVE PHOSPHORYLATION). Flavoproteins are also capable of directly oxidizing various substrates and detaching from them hydrogen atoms, which are then transferred onto oxygen either immediately (for example, xanthine oxidase) or through the chain of transfer of electrons (for example, succinate dehydrogenase).

Flavoproteins are abundant in nature; they participate in the catabolism of major classes of organic compounds in the cells of animals, plants, and microorganisms.


Lehninger, A. Biokhimiia. Moscow, 1976. (Translated from English.)


The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
It is hypothesized that the antioxidant functionality of riboflavin has been complemented by way of direct free radical scavenging as well as its nature of being a part of the flavoprotein family, such as glutathione reductase.
[3] Nonstandard abbreviations: MADD, multiple acyl-CoA dehydrogenase deficiency; ETF, electron transfer flavoprotein; ETF:QO, ETF dehydrogenase; GA II, glutaric aciduria type II; GAI, glutaric aciduria type I; D-2-HGDH, D-2-hydroxyglutaric acid dehydrogenase; C4, butyrylcarnitine; C5, 2-methylbutyrylcarnitine; C5-DC, glutarylcarnitine; C6, hexanoylcarnitine; C8, octanoylcarnitine; C12, dodecanoylcarnitine; C14, myristoylcarnitine; C16, palmitoylcarnitine.
Vallon, "New sequence motifs in flavoproteins: evidence for common ancestry and tools to predict structure," Proteins, vol.
Cryptochromes are flavoproteins and act as blue-light receptors in numerous species on the earth, which have high sequences homology to photolyases (Sancar, 2003; LIN & Shalitin, 2003; LIN, 2000).
Monoamine oxidases (MAOs) are flavoproteins which catalyze the oxidative deamination of a variety of neurotransmitters, such as noradrenaline, dopamine, and serotonin, as well as different exogenous and endogenous amines (i.e., tyramine, benzylamine, etc.) to their corresponding aldehydes.
Chemistry and Biochemistry of Flavoproteins. Boca Raton, Fla: CRC Press; 1990:229-297.
Putative human blue-light photoreceptors hCRYl and hCRY2 are flavoproteins. Biochemistry 35: 13871-13877.
Mitochondrial uncoupling was associated with upregulated FAO genes and electron transfer flavoproteins [80].
Iron is also present in the composition of flavoproteins and heme proteins catalase and peroxidase (found in erythrocytes and hepatocytes).
Flavoproteins autofluoresce, emitting light in the same region as fluorescein and limiting the use of this fluorophore in samples rich in flavoproteins (e.g., liver and kidney tissues).
However, none of these former studies were performed with the native forms of the human MAO flavoproteins naturally expressed in brain or peripheral tissues.