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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.


Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan[1][2][3] and Howard S. Mason from the US.[4][5] Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance."[6]

Chemical Makeup[edit]

Oxygenases consist of both constitutive and inducible isozymes (HO-1, HO-2). These constitute a major intracellular source of iron and carbon monoxide[7]


There are two types of oxygenases:

Among the most important monooxygenases are the cytochrome P450 oxidases, responsible for breaking down numerous chemicals in the body.


  1. ^ Hayaishi et al. (1955) Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451
  2. ^ Sligar SG, Makris TM, Denisov IG (2005). "Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis". Biochem. Biophys. Res. Commun. 338 (1): 346–54. doi:10.1016/j.bbrc.2005.08.094. PMID 16139790.
  3. ^ Hayaishi O (2005). "An odyssey with oxygen". Biochem. Biophys. Res. Commun. 338 (1): 2–6. doi:10.1016/j.bbrc.2005.09.019. PMID 16185652.
  4. ^ Mason HS, Fowlks WK, Peterson E (1955). "Oxygen transfer and electron transport by the phenolase complex". J. Am. Chem. Soc. 77 (10): 2914–2915. doi:10.1021/ja01615a088.
  5. ^ Waterman MR (2005). "Professor Howard Mason and oxygen activation". Biochem. Biophys. Res. Commun. 338 (1): 7–11. doi:10.1016/j.bbrc.2005.08.120. PMID 16153596.
  6. ^ "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.
  7. ^ SW, Ryter; J, Alam (April 2006). "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications". Physiol Rev. Department of Medicine, Division of Pulmonary, Allergy, and Critical Care Medicine, The University of Pittsburgh School of Medicine. 86: 583–650. doi:10.1152/physrev.00011.2005. PMID 16601269.
  8. ^ Bugg TDH (2003). "Dioxygenase enzymes: catalytic mechanisms and chemical models". Tetrahedron. 59 (36): 7075–7101. doi:10.1016/S0040-4020(03)00944-X.