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 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.
