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]
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]
^SW, Ryter; J, Alam (April 2006). "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications". Physiol Rev. 86 (2). Department of Medicine, Division of Pulmonary, Allergy, and Critical Care Medicine, The University of Pittsburgh School of Medicine: 583–650. doi:10.1152/physrev.00011.2005. PMID16601269.
^Bugg TDH (2003). "Dioxygenase enzymes: catalytic mechanisms and chemical models". Tetrahedron. 59 (36): 7075–7101. doi:10.1016/S0040-4020(03)00944-X.
^Hayaishi et al. (1955) Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451
^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. PMID16139790.
^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.
