title: Enzyme-substrate complementarity governs access to a cationic reaction manifold in the P450(BM3)-catalysed oxidation of cyclopropyl fatty acids.
abstract: The products of cytochrome P450(BM3)-catalysed oxidation of cyclopropyl-containing dodecanoic acids are consistent with the presence of a cationic reaction intermediate, which results in efficient dehydrogenation of the rearranged probes by the enzyme. These results highlight the importance of enzyme-substrate complementarity, with a cationic intermediate occurring only when the probes used begin to diverge from ideal substrates for this enzyme. This also aids in reconciling literature reports supporting the presence of cationic intermediates with certain cytochrome P450 enzyme/substrate pairs.
authors.affiliation: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia Brisbane, 4072, Australia.
authors.forename: Max J
authors.initials: MJ
authors.lastname: Cryle
authors.forename: Patricia Y
authors.initials: PY
authors.lastname: Hayes
authors.forename: James J
authors.initials: JJ
authors.lastname: De Voss
mesh_terms: D002384:Catalysis; D002412:Cations / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D005227:Fatty Acids / Q000737:chemistry*; D006900:Hydroxylation; D007700:Kinetics; D007850:Lauric Acids / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction
chemical_list: D002412:Cations; D005227:Fatty Acids; D007850:Lauric Acids; D003577:Cytochrome P-450 Enzyme System