Cytochrome P450cam catalyzed epoxidation of dehydrocamphor

Michael H. Gelb, Pentti Malkonen, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review


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 languageEnglish (US)
Pages (from-to)853-858
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Feb 11 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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