title: Expanding the substrate scope and reactivity of cytochrome P450 OleT.
abstract: The efficient hydrogen peroxide-dependent hydroxylation and epoxidation of hydrocarbons is catalysed by a P450 fatty acid decarboxylase (OleT) active-site variant. The introduction of an acidic functionality in the protein framework circumvents the necessity for a carboxylate that is typically provided by the substrate for efficient H2O2 heterolysis. Spectroscopic and turnover studies show that the mutation eliminates the binding and metabolism of prototypical fatty acid substrates, but permits the oxidation of a broad range of inert hydrocarbon substrates.
authors.affiliation: University of South Carolina, Department of Chemistry and Biochemistry, 631 Sumter Street, Columbia, SC 29208, USA.
authors.forename: Chun H
authors.initials: CH
authors.lastname: Hsieh
authors.affiliation: University of South Carolina, Department of Chemistry and Biochemistry, 631 Sumter Street, Columbia, SC 29208, USA. Electronic address: makrist@mailbox.sc.edu.
authors.forename: Thomas M
authors.initials: TM
authors.lastname: Makris
mesh_terms: D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain / Q000235:genetics; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040141:Staphylococcaceae / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D005227:Fatty Acids; D011994:Recombinant Proteins; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide
keywords: Compound I; Cytochrome P450; C–H functionalization; Monooxygenase; Oxidative decarboxylation; Oxygen activation