ArticleBiochemistry2009
Kinetic isotope effects in hydroxylation reactions effected by cytochrome P450 compounds I implicate multiple electrophilic oxidants for P450-catalyzed oxidations.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Local Electric Fields Originate Unusual Kinetic Isotope Effects in the Hydrogen Abstraction Reactions of the Functionally Analogous P450 and TauD Enzymes.Journal of the American Chemical Society · 2025Article
- The Oxidation Cascade of a Rare Multifunctional P450 Enzyme Involved in Asperterpenoid A Biosynthesis.Frontiers in chemistry · 2021Article
- Functioning of drug-metabolizing microsomal cytochrome P450s: In silico probing of proteins suggests that the distal heme 'active site' pocket plays a relatively 'passive role' in some enzyme-substrate interactions.In silico pharmacology · 2016Article
- The diverse chemistry of cytochrome P450 17A1 (P450c17, CYP17A1).The Journal of steroid biochemistry and molecular biology · 2015Review
- Reactive intermediates in cytochrome p450 catalysis.The Journal of biological chemistry · 2013Review
- Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.Archives of biochemistry and biophysics · 2011Review
- Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates H(peroxo) and Q proceed by distinct mechanisms.Biochemistry · 2010Article
- Mechanisms of peroxynitrite interactions with heme proteins.Inorganic chemistry · 2010Article
- Hydrocarbon hydroxylation by cytochrome P450 enzymes.Chemical reviews · 2010Review
- Kinetics and activation parameters for oxidations of styrene by Compounds I from the cytochrome P450(BM-3) (CYP102A1) heme domain and from CYP119.Biochemistry · 2009Article
- Quantitative production of compound I from a cytochrome P450 enzyme at low temperatures. Kinetics, activation parameters, and kinetic isotope effects for oxidation of benzyl alcohol.Journal of the American Chemical Society · 2009Article
- Kinetics of oxidation of benzphetamine by compounds I of cytochrome P450 2B4 and its mutants.Journal of the American Chemical Society · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Kinetic isotope effects were measured for oxidations of (S,S)-2-(p-trifluoromethylphenyl)cyclopropylmethane containing zero, two, and three deuterium atoms on the methyl group by Compounds I from the cytochrome P450 enzymes CYP119 and CYP2B4 at 22 degrees C. The oxidations displayed saturation kinetics, which permitted solution of both binding constants (K(bind)) and first-order oxidation rate constants (k(ox)) for both enzymes with the three substrates. The binding constant for CYP2B4 Compound I was about 1 order of magnitude greater than that for CYP119 Compound I, but the oxidation rate constants were similar for the two. In oxidations of 1-d(0), k(ox) = 10.4 s(-1) for CYP119 Compound I, and k(ox) = 12.4 s(-1) for CYP2B4 Compound I. Primary kinetic isotope effects (P) and secondary kinetic isotope effects (S) were obtained from the results with the three isotopomers. The primary KIEs were large, P = 9.8 and P = 8.9 for CYP119 and CYP2B4 Compounds I, respectively, and the secondary KIEs were small and normal, S = 1.07 and S = 1.05, respectively. Large intermolecular KIEs for 1-d(0) and 1-d(3) of k(H)/k(D) = 11.2 and 9.8 found for the two Compounds I contrast with small intermolecular KIEs obtained previously for the same substrate in P450-catalyzed oxidations; these differences suggest that a second electrophilic oxidant, presumably iron-complexed hydrogen peroxide, is important in cytochrome P450 oxidations under turnover conditions.
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