Efficient biocatalytic C–H bond oxidation: an engineered heme-thiolate peroxygenase from a thermostable cytochrome P450
Alecia R. Gee, Isobella S. J. Stone, Tegan P. Stockdale, Tara L. Pukala, James J. De Voss, Stephen G. Bell
Abstract
A highly sought after reaction in chemical synthesis is the activation of unactivated carbon-hydrogen bonds. We demonstrate the hydroxylation of fatty acids using an engineered thermostable archaeal cytochrome P450 enzyme. By replacing a seven amino acid section of the I-helix, the nicotinamide cofactor-dependent monooxygenase was converted into a hydrogen peroxide using peroxygenase, enabling the efficient biocatalytic oxidation of C-H bonds at room temperature to 90 °C.
Topics & Concepts
HemeChemistryHemeproteinBiocatalysisCytochrome P450CytochromeCombinatorial chemistryStereochemistryOrganic chemistryEnzymeBiochemistryCatalysisReaction mechanismMetal-Catalyzed Oxygenation MechanismsCatalytic C–H Functionalization MethodsSynthesis and Catalytic Reactions