Kinetics of Two-Electron Oxidations by the Compound I Derivative of Chloroperoxidase, a Model for Cytochrome P450 Oxidants

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Abstract
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.