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Chem. Rev. 2005, 105, 2253−2277 2253
Structure and Chemistry of Cytochrome P450
Ilia G. Denisov,† Thomas M. Makris,† Stephen G. Sligar,*†,‡ and Ilme Schlichting*,§
Departments of Biochemistry and Chemistry, Center for Biophysics and Computational Biology, University of Illinois,
Urbana−Champaign, Illinois 61801 and Department of Biomolecular Mechanisms, Max Planck Institut fu¨r Medizinische Forschung,
Jahnstrasse 29, 69 120 Heidelberg, Germany
Received October 28, 2004
Contents catechol to muconic acid by oxidative cleavage.1 He
named this biological catalyst “pyrocatechase”, which
1. Introduction 2253
proved to be the landmark discovery of an enzyme
2. Active-Site Structure of P450 Enzymes 2256 that incorporated atmospheric dioxygen into the
3. Enzymatic Reaction Cycle of Cytochrome P450 2256 carbon chain of the substrate, thereby initiating
3.1. Substrate Binding 2257 cleavage of the benzene ring. This review of the
3.2. Iron Spin Shift and the Heme Redox 2258 oxygenase cytochrome P450 is dedicated to Dr.
Potential Hayaishi and his pioneering discovery in what is now
3.3. Oxygen Complex
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