Year: 2013
Type: review
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.
Source: Journal of Biological Chemistry
Authors: F. Peter Guengerich, Andrew W. Munro
Institutions: Vanderbilt University, University of Manchester
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: Novel routes to catalytic intermediates in the cytochrome P450 catalytic cycle, Metabolism of Carcinogens and Drugs by Human P450s, Elucidating and exploiting cytochrome P450 TxtE-catalysed tryptophan nitration in thaxtomin phytotoxin biosynthesis, Directed evolution approaches to generation of an industrially applicable biocatalyst, Metabolism of Carcinogens and Drugs by Human P450s, Center in Molecular Toxicology, Molecular reconstruction of flavocytochrome P450 BM3, A fragment based screening approach to rationalizing M. tuberculosis P450 molecular selectivity, Characterization of a superior biocatalyst for pravastatin production, G9000098251
OpenAlex ID: W2047259762