Journal
COMPTES RENDUS CHIMIE
Volume 10, Issue 4-5, Pages 392-413Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.crci.2006.11.001
Keywords
hemeproteins; bioniorganic chemistry; drug metabolism; biomimetic systems; dioxygen; iron porphyrins
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Since their discovery in the 1960s, cytochrome P450-dependent monooxygenases have very much attracted the interest of chemists because of their ability to catalyze the selective transfer of an oxygen atom from O-2 to very diverse substrates including alkanes. The huge number of studies performed during these last 30 years on P450s themselves and on iron porphyrin models has led to a detailed understanding of the oxidations catalyzed by iron porphyrins and hemeproteins in general, and to the design of many bioinspired oxidation catalysts. This article gives an overview of what were the main contributions of metalloporphyrin model studies to the fields of P450 chemistry and oxidation catalysis, through a brief comparative history of the development of our knowledge on cytochrome P450 and on the development and use of metalloporphyrin models.
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