Oxygenase
An oxygenase is any
substrate by transferring the oxygen from molecular oxygen O2 (as in air) to it. The oxygenases form a class of oxidoreductases; their EC number
is EC 1.13 or EC 1.14.
Structure
Most oxygenases contain either a metal, usually iron, or an organic cofactor, usually flavin. These cofactors interact with O2, leading to its transfer to substrate.[1]
Oxygenases constitute a major intracellular source of iron and carbon monoxide[2]
Mechanism
Two types of oxygenases are recognized:
- mixed function oxidase, transfer one oxygen atom to the substrate, and reduce the other oxygen atom to water.
- Dioxygenases, or oxygen transferases, incorporate both atoms of molecular oxygen (O2) into the product(s) of the reaction.[3]
Among the most common monooxygenases are the
cytochrome P450 oxidases
, responsible for breaking down numerous chemicals in the body.
History
Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan[4][5][6] and Howard S. Mason from the US.[7][8] Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance."[9]
References
- S2CID 25377247.
- PMID 16601269.
- .
- ^ Hayaishi et al. (1955) Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451
- PMID 16139790.
- PMID 16185652.
- .
- PMID 16153596.
- ^ "The Medicine Prize Committee unanimously decided that the Wolf Prize in Medicine for 1986 be awarded to Osamu Hayaishi". Wolf Foundation. Retrieved May 12, 2014.
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