Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle

Authors

Piotr J. Mak, Marquette UniversityFollow
Ilia G. Denisov, University of Illinois at Urbana-Champaign
Doreen Victoria, University of Illinois at Urbana-Champaign
Thomas M. Makris, University of Illinois at Urbana-Champaign
Tianjing Deng, Marquette University
Stephen G. Sligar, University of Illinois at Urbana-Champaign
James R. Kincaid, Marquette UniversityFollow

Document Type

Article

Language

eng

Format of Original

2 p.

Publication Date

2007

Publisher

American Chemical Society

Source Publication

Journal of the American Chemical Society

Source ISSN

0002-7863

Original Item ID

DOI: 10.1021/ja071426h

Abstract

The resonance Raman spectra of the hydroperoxo complex of camphor-bound CYP101 have been obtained by cryoradiolytic reduction of the oxygenated ferrous form that had been rapidly frozen in water/glycerol frozen solution; EPR spectroscopy was employed to confirm the identity of the trapped intermediate. The ν(O−O) mode, appearing at 799 cm^-1, is observed for the first time in a peroxo-heme adduct. It is assigned unambiguously by employing isotopomeric mixtures of oxygen gas containing 50% ¹⁶O¹⁸O, confirming the presence of an intact O−O fragment. The ν(Fe−O) mode is observed at 559 cm^-1 (H₂O). Furthermore, both modes shift down by 3 cm^-1, documenting the formulation as a hydroperoxo complex, in agreement with EPR data.

Comments

Accepted version. Journal of the American Chemical Society, Vol. 129, No. 20 (2007): 6382-6383. DOI. © 2007 American Chemical Society. Used with permission.

Recommended Citation

Mak, Piotr J.; Denisov, Ilia G.; Victoria, Doreen; Makris, Thomas M.; Deng, Tianjing; Sligar, Stephen G.; and Kincaid, James R., "Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle" (2007). Chemistry Faculty Research and Publications. 405.
https://epublications.marquette.edu/chem_fac/405