oxygenase
{{Short description|Enzyme}}
File:EC_1.13.11.11_Tryptophan_2,3-dioxygenase_-_PDB_id_1yw0_-_EBI.jpg
An oxygenase is any enzyme that oxidizes a 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.{{cite journal |doi=10.1007/s00253-010-2455-0|title=Cofactor-independent oxidases and oxygenases |year=2010 |last1=Fetzner |first1=Susanne |last2=Steiner |first2=Roberto A. |journal=Applied Microbiology and Biotechnology |volume=86 |issue=3 |pages=791–804 |pmid=20157809 |s2cid=25377247 }}
Oxygenases constitute a major intracellular source of iron and carbon monoxide{{cite journal |last1=SW |first1=Ryter |last2=J |first2=Alam |date=April 2006 |title=Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. |pmid=16601269 |journal= Physiol Rev|publisher=Department of Medicine, Division of Pulmonary, Allergy, and Critical Care Medicine, The University of Pittsburgh School of Medicine |volume= 86|issue=2 |pages= 583–650|doi= 10.1152/physrev.00011.2005}}
Mechanism
Two types of oxygenases are recognized:
- Monooxygenases, or 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.{{cite journal |author=Bugg TDH |title=Dioxygenase enzymes: catalytic mechanisms and chemical models |journal=Tetrahedron |volume=59 |pages=7075–7101 |year=2003 |doi=10.1016/S0040-4020(03)00944-X |issue=36}}
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 JapanHayaishi et al. (1955) Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451{{cite journal |vauthors=Sligar SG, Makris TM, Denisov IG |title=Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue=1 |pages=346–54 |year=2005 |pmid=16139790 |doi=10.1016/j.bbrc.2005.08.094}}{{cite journal |author=Hayaishi O |title=An odyssey with oxygen |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue=1 |pages=2–6 |year=2005 |pmid=16185652 |doi=10.1016/j.bbrc.2005.09.019}} and Howard S. Mason from the US.{{cite journal |vauthors=Mason HS, Fowlks WK, Peterson E | year = 1955 | title = Oxygen transfer and electron transport by the phenolase complex | journal = J. Am. Chem. Soc. | volume = 77 | issue = 10| pages = 2914–2915 | doi=10.1021/ja01615a088}}{{cite journal |author=Waterman MR |title=Professor Howard Mason and oxygen activation |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue=1 |pages=7–11 |year=2005 |pmid=16153596 |doi=10.1016/j.bbrc.2005.08.120}} Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance."{{cite web|title=The Medicine Prize Committee unanimously decided that the Wolf Prize in Medicine for 1986 be awarded to Osamu Hayaishi|url=http://www.wolffund.org.il/index.php?dir=site&page=winners&cs=495&language=eng|archive-url=https://web.archive.org/web/20140714212813/http://www.wolffund.org.il/index.php?dir=site&page=winners&cs=495&language=eng|url-status=dead|archive-date=July 14, 2014|publisher=Wolf Foundation|access-date=May 12, 2014}}
References
{{Enzymes}}
{{Monooxygenases}}
{{Dioxygenases}}
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