Low-temperature rapid-scan detection of reactive intermediates in epoxidation reactions catalyzed by a new enzyme mimic of cytochrome p450.
The use of synthetic iron(III) porphyrins as models for heme-type catalysts in biomimetic cytochrome P450 research has provided valuable information on the nature and reactivity of intermediates produced in the "peroxide shunt" pathway. This article reports spectroscopic detection of reactive intermediates formed in the epoxidation reaction of cis-stilbene with m-chloroperoxybenzoic acid catalyzed by a new mimic of cytochrome P450 with a substituted RSO3- group (1). The application of low-temperature rapid-scan stopped-flow techniques enabled the determination of equilibrium and rate constants for the formation and decay of all intermediates in the catalytic cycle of 1, including the rate constant for the formation (1*+)FeIV=O and for oxygen transfer to the substrate. Noteworthy, the reaction of (1*+)FeIV=O with cis-stilbene leads to an almost complete re-formation (95%) of the starting complex 1. The results show that complex 1 is a valuable catalyst with promising properties for further applications in a biomimetic approach toward mimicking oxygenation reactions of cytochrome P450.
Hessenauer-Ilicheva
Natalya
N
Institute for Inorganic Chemistry, University of Erlangen-Nürnberg, Egerlandstrasse 1, 91058 Erlangen, Germany.
Franke
Alicja
A
Meyer
Dominik
D
Woggon
Wolf-D
WD
van Eldik
Rudi
R
D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D002723:Chlorobenzoates / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004852:Epoxy Compounds / Q000737:chemistry*; D007700:Kinetics; D015394:Molecular Structure; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
D002723:Chlorobenzoates; D004852:Epoxy Compounds; D003577:Cytochrome P-450 Enzyme System; C000433:3-chloroperbenzoic acid