Kinetics of two-electron oxidations by the compound I derivative of chloroperoxidase, a model for cytochrome P450 oxidants.
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ABSTRACT:
SUBMITTER: Zhang R
PROVIDER: S-EPMC2535770 | biostudies-literature | 2006 Jun
REPOSITORIES: biostudies-literature
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Kinetics of two-electron oxidations by the compound I derivative of chloroperoxidase, a model for cytochrome P450 oxidants.
Zhang Rui R Nagraj Nandini N Lansakara-P Dharmika S P DS Hager Lowell P LP Newcomb Martin M
Organic letters 20060601 13
[structure: see text] Rate constants for two-electron oxidation reactions of Compound I from chloroperoxidase (CPO) with a variety of substrates were measured by stopped-flow kinetic techniques. The thiolate ligand of CPO Compound I activates the iron-oxo species with the result that oxidation reactions are 2 to 3 orders of magnitude faster than oxidations by model iron(IV)-oxo porphyrin radical cations containing weaker binding counterions. ...[more]
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