title: Selective oxygen transfer catalysed by heme peroxidases: synthetic and mechanistic aspects.
abstract: The synthetic and mechanistic aspects of the use of heme peroxidases as functional mimics of the cytochrome P450 monooxygenases in oxygen-transfer reactions have been described. The chloroperoxidase from Caldariomyces fumago (CPO) is the catalyst of choice in sulfoxidation, hydroxylation and epoxidation on account of its high activity and enantioselectivity. Other heme peroxidases were less active by orders of magnitude; protein engineering has resulted in impressive improvements but even the most active mutant was still at least an order of magnitude less active than CPO. The 'oxygen-rebound' mechanisms of oxygen transfer mediated by heme enzymes - as originally conceived - have proved to be untenable. Dual pathway mechanisms, via oxoferryl species that insert oxygen as well as iron hydroperoxide species that insert OH(+), have been proposed that accommodate all of the known experimental data.
authors: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
authors: F
authors: F
authors: van Rantwijk
authors: R A
authors: RA
authors: Sheldon
mesh_terms: D002384:Catalysis; D004579:Electron Transport; D006418:Heme / Q000737:chemistry; D010100:Oxygen / Q000378:metabolism*; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D006418:Heme; D010544:Peroxidases; D010100:Oxygen