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flavoprotein

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Definitions of flavoprotein in various dictionaries:

Any of a group of enzymes containing flavin bound to protein and acting as dehydrogenation catalysts in biological reactions.

FLAVOPROTEIN - Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN)...

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Any of a group of enzymes containing flavin bound to protein and acting as dehydrogenation catalysts in biological reactions.
Any of a class of conjugated proteins that contain flavins and are involved in oxidation reactions in cells.

Flavoprotein might refer to
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN). * Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence, removal of radicals contributing to oxidative stress, photosynthesis, DNA repair, and apoptosis. The spectroscopic properties of the flavin cofactor make it a natural reporter for changes occurring within the active site; this makes flavoproteins one of the most-studied enzyme families. * Flavoproteins have either an FMN or FAD molecule as a prosthetic group. This prosthetic group is generally tightly bound (see example adrenodoxin reductase wherein the FAD is deeply buried in the enzyme). * About 5-10% of flavoproteins have a covalently linked FAD, but these enzymes have stronger redox power. In some instances, FAD can provide structural support for active sites or provide stabilization of intermediates during catalys

Flavoprotein might refer to

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).
* Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence, removal of radicals contributing to oxidative stress, photosynthesis, DNA repair, and apoptosis. The spectroscopic properties of the flavin cofactor make it a natural reporter for changes occurring within the active site; this makes flavoproteins one of the most-studied enzyme families.
* Flavoproteins have either an FMN or FAD molecule as a prosthetic group. This prosthetic group is generally tightly bound (see example adrenodoxin reductase wherein the FAD is deeply buried in the enzyme).
* About 5-10% of flavoproteins have a covalently linked FAD, but these enzymes have stronger redox power. In some instances, FAD can provide structural support for active sites or provide stabilization of intermediates during catalys

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