In addition to the normal 5-exo-hydroxylation of camphor, bacterial cytochrome P450 is shown to carry out the facile epoxidation of dehydrocamphor to give exo-5,6-epoxycamphor. A detailed kinetic study of the reaction demonstrates that epoxidation and hydroxylation reactions occur with nearly identical rates both in the reconstituted system containing flavoprotein dehydrogenase, iron-sulfur protein, and NADH as well as in the single turnover reaction beginning with ferrous, oxygenated cytochrome P450. Dehydrocamphor is not a suicide substrate for the enzyme since competent enzyme remains after several thousand reaction cycles per P450 molecule.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Feb 11 1982|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology