title: Cytochrome P450: nature's most versatile biological catalyst.
abstract: The author describes studies that led to the resolution and reconstitution of the cytochrome P450 enzyme system in microsomal membranes. The review indicates how purification and characterization of the cytochromes led to rigorous evidence for multiple isoforms of the oxygenases with distinct chemical and physical properties and different but somewhat overlapping substrate specificities. Present knowledge of the individual steps in the P450 and reductase reaction cycles is summarized, including evidence for the generation of multiple functional oxidants that may contribute to the exceptional diversity of the reactions catalyzed.
authors.affiliation: Department of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor 48109, USA. mjcoon@umich.edu
authors.forename: Minor J
authors.initials: MJ
authors.lastname: Coon
mesh_terms: D000818:Animals; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System