X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry

Kari L Stone; Rachel K Behan; Michael T Green

doi:10.1073/pnas.0507069102

X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry

Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16563-5. doi: 10.1073/pnas.0507069102. Epub 2005 Nov 7.

Authors

Kari L Stone¹, Rachel K Behan, Michael T Green

Affiliation

¹ Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

Abstract

We report the structural characterization of a thiolate-ligated ferryl radical. Using x-ray absorption spectroscopy, we examined chloroperoxidase (CPO) compound I (CPO-I). Our results indicate that CPO-I is an authentic ferryl species with an Fe-O bond of 1.65 A. Axial-ligand interactions result in a remarkably long 2.48-A Fe-S bond. Analogous forms of cytochrome P450 and CPO have been shown to possess virtually identical coordination environments. Thus, it seems likely that our findings provide a good structural description of the elusive P450-I.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Chloride Peroxidase / chemistry*
Cytochrome P-450 Enzyme System / chemistry*
Protein Conformation
Spectrum Analysis
X-Rays

Substances

Cytochrome P-450 Enzyme System
Chloride Peroxidase