期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 12, 页码 9641-9644出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C100745200
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资金
- NIGMS NIH HHS [GM31756, GM33775] Funding Source: Medline
The kinetics of formation and breakdown of the putative active oxygenating intermediate in cytochrome P450, a ferryl-oxo-(pi) porphyrin cation radical (Compound 1), 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-(pi) 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) x :10(5) m(-1) s(-1) at pH 7.0, 4 degreesC, 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 s(-1), 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.
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