NDLI: Direct Comparison of the Reactivity of Model Complexes for Compounds 0, I, and II in Oxygenation, Hydrogen-Abstraction, and Hydride-Transfer Processes

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Direct Comparison of the Reactivity of Model Complexes for Compounds 0, I, and II in Oxygenation, Hydrogen-Abstraction, and Hydride-Transfer Processes

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Direct Comparison of the Reactivity of Model Complexes for Compounds 0, I, and II in Oxygenation, Hydrogen-Abstraction, and Hydride-Transfer Processes

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hessenauer-ilicheva, Natalya Fertinger, Christoph Franke, Alicja Van Eldik, Rudi
Description	Author Affiliation: Fertinger C ( Inorganic Chemistry, Department of Chemistry and Pharmacy, University of Erlangen-Nuremberg, Egerlandstrasse 1, 91058 Erlangen, Germany.)
Abstract	The iron(III) meso-tetramesitylporphyrin complex is a good biomimetic to study the catalytic reactions of cytochrome P450. All of the three most discussed reactive intermediates concerning P450 catalysis (namely, Cpd 0, Cpd I, and Cpd II) can be selectively produced, identified, and stabilized for many minutes in solution at low temperature by choosing appropriate reaction conditions. In this way, their reactivity against various substrates was determined by utilizing low-temperature rapid-scan UV/Vis spectroscopy. Since all reactive intermediates are derived from a single model complex, the results of these kinetic measurements provide for the first time a full comparability of the determined rate constants for the three intermediates. The rate constants reveal a significant dependence of the reactivity on the type of reaction (e.g., oxygenation, hydrogen abstraction, or hydride transfer), which closely correlates with the chemical nature of Cpds 0, I, and II. The detailed knowledge of the reactivity of these intermediates provides a valuable tool to evaluate their particular role in biological systems.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	48
Volume Number	15
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2009-12-14
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Cytochrome P-450 Enzyme System Chemistry Hydrogen Metalloporphyrins Kinetics Molecular Structure Oxidation-Reduction Substrate Specificity Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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