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J. Biol. Chem., Vol. 277, Issue 12, 9641-9644, March 22, 2002
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From the Departments of Biochemistry, Chemistry, and the
College of Medicine, University of Illinois,
Urbana, Illinois 61801
The kinetics of formation and breakdown of the
putative active oxygenating intermediate in cytochrome P450, a
ferryl-oxo-(
ACCELERATED PUBLICATION
Kinetic Characterization of Compound I Formation in the
Thermostable Cytochrome P450 CYP119*
) porphyrin cation radical (Compound I), have been
analyzed in the reaction of a thermostable P450, CYP119, with
meta-chloroperoxybenzoic acid (m-CPBA). Upon
rapid mixing of m-CPBA with the ferric form of CYP119, an
intermediate with spectral features characteristic of a
ferryl-oxo-() porphyrin cation radical was clearly observed and
identified by the absorption maxima at 370, 610, and 690 nm. The rate
constant for the formation of Compound I was 3.20 (±0.3) × 105 M
1 s1 at pH
7.0, 4 °C, and this rate decreased with increasing pH. Compound I of
CYP119 decomposed back to the ferric form with a first order rate
constant of 29.4 ± 3.4 s1, which increased with
increasing pH. These findings form the first kinetic analysis of
Compound I formation and decay in the reaction of m-CPBA
with ferric P450.
*
This work was supported by National Institutes of Health
Grants GM 31756 and GM 33775.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: School of Molecular
and Cellular Biology, 505 S. Goodwin Ave., University of Illinois at
Champaign-Urbana, Urbana, IL 61801. Tel.: 217-244-7395; Fax: 217-265-4073; E-mail: s-sligar@uiuc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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