| Literature DB >> 23632016 |
F Peter Guengerich1, Andrew W Munro.
Abstract
Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high-valent iron-oxygen complex (FeO(3+)), to explain seemingly unusual reactions, including ring couplings, ring expansion and contraction, and fusion of substrates. Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H. In some cases, P450s are fused to protein partners. Other P450s catalyze non-redox isomerization reactions. A number of permutations on the P450 theme reveal the diversity of cytochrome P450 form and function.Entities:
Keywords: Cytochrome P450; Enzyme Catalysis; Enzyme Mechanisms; Flavin; Heme; Natural Products; Oxidation-Reduction
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Year: 2013 PMID: 23632016 PMCID: PMC3682512 DOI: 10.1074/jbc.R113.462275
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157