title: Bio-organic chemistry and cytochrome P-450-dependent catalysis.
abstract: This review presents current ideas, models and experimental data relating to the precise chemistry that links the transition metal active centre of cytochrome P-450 systems, the unactivated alkane substrate and the triplet atmospheric dioxygen molecule. Aspects considered include the hypervalent transition metal, the reductive activation of the dioxygen molecule by two electrons as an intermediate in the four-equivalent oxidase mechanism, and the details of carbon-hydrogen and carbon-carbon fragmentation. Studies of the microbial camphor 5-exo hydroxylase system are used to exemplify the principles discussed.
mesh_terms: D000818:Animals; D001711:Biotransformation; D002164:Camphor / Q000031:analogs & derivatives / Q000378:metabolism; D019475:Camphor 5-Monooxygenase; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006420:Hemeproteins / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000378:metabolism; D008956:Models, Chemical; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D010105:Oxygenases / Q000378:metabolism
chemical_list: D006420:Hemeproteins; D006418:Heme; D009249:NADP; D002164:Camphor; C020453:beta-pericyclocamphanone; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D010105:Oxygenases; D019475:Camphor 5-Monooxygenase