Epoxidation of Olefins by Hydroperoxo−Ferric Cytochrome P450

Citations Over TimeTop 10% of 2003 papers

Abstract

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.

Related Papers

• → Studies on the nature of the racemic modifications of optically active compounds in the solid state(1952)2 cited
• → On Japanese camphor—its preparation experiments and analyses of the camphor oil(1884)
• Determination of Camphor in Dongchuang Ointment by GC(2008)
• Determination of camphor in camphor cream by UV spectrophotometry(2004)
• Determination of camphor in compound camphor spirit by high-performance liquid chromatography(2013)