Epoxidation of olefins by hydroperoxo-ferric cytochrome P450.
The T252A mutant of cytochrome P450cam is unable to form the oxoferryl "active oxygen" intermediate, as judged by its inability to hydroxylate its normal substrate, camphor. In the present study, we demonstrate that T252A P450cam is nonetheless able to epoxidize olefins, due to the action of a second oxidant. However, as shown in earlier radiolytic studies and by the ability of T252A to reduce dioxygen to hydrogen peroxide, the mutant retains the ability to form the hydroperoxo-ferric reaction cycle intermediate. The present results provide strong evidence that hydroperoxo-ferric P450 can serve as a second electrophilic oxidant capable of olefin epoxidation.
Jin
Shengxi
S
Department of Chemistry and Biochemistry and the School of Medicine, University of South Carolina, Columbia, South Carolina 29208, USA.
Makris
Thomas M
TM
Bryson
Thomas A
TA
Sligar
Stephen G
SG
Dawson
John H
JH
D000473:Alkanes / Q000737:chemistry* / Q000378:metabolism; D019475:Camphor 5-Monooxygenase / Q000737:chemistry* / Q000378:metabolism; D004852:Epoxy Compounds / Q000138:chemical synthesis* / Q000378:metabolism; D005290:Ferric Compounds / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D016958:Pseudomonas putida / Q000201:enzymology
D000473:Alkanes; D004852:Epoxy Compounds; D005290:Ferric Compounds; D019475:Camphor 5-Monooxygenase