Kinetics of two-electron oxidations by the compound I derivative of chloroperoxidase, a model for cytochrome P450 oxidants.
[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.
Zhang
Rui
R
Department of Chemistry, University of Illinois at Chicago, 60607, USA.
Nagraj
Nandini
N
Lansakara-P
Dharmika S P
DS
Hager
Lowell P
LP
Newcomb
Martin
M
D002711:Chloride Peroxidase / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry; D007700:Kinetics; D008665:Metalloporphyrins / Q000737:chemistry; D008954:Models, Biological; D016877:Oxidants / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D008665:Metalloporphyrins; D016877:Oxidants; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D002711:Chloride Peroxidase