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Synlett 2005(4): 675-684  
DOI: 10.1055/s-2005-863724
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© Georg Thieme Verlag Stuttgart · New York

New Synthetic Models of Cytochrome P450: How Different Are They from the Natural Species?

Sebastian Kozucha, Tycho Leifelsb, Dominik Meyerb, Laura Sbaraglib, Sason Shaik*a, Wolf-D. Woggon*b
a Department of Organic Chemistry and The Lise Meitner-Minerva Center for Computational Quantum Chemistry, Givat Ram Campus, Jerusalem 91904, Israel
b Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056 Basel, Switzerland
Fax: +41(61)2671102; e-Mail: wolf-d.woggon@unibas.ch;
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Publication History

Received 3 December 2004
Publication Date:
22 February 2005 (online)

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Abstract

Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3 - ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3 - to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.

Key words

catalysis - enzyme models - DFT calculations - heme-thiolate proteins - iron porphyrins

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