Abstract
The heme-thiolate enzymes such as cytochrome P450 (CYP), chloroperoxidase (CPO), P450BSβ and recently discovered peroxygenase, AaeAPO, catalyze a variety of crucial oxidative reactions. Among them, the activation of inert hydrocarbons via C–H bond hydroxylation plays an important role in biology. These reactions are involved in the biosynthesis of steroids, the degradation of xenobiotics, the metabolism of drugs and so on. Understanding the mechanisms of these reactions provides us guidelines for the design of new catalysts and the application of biocatalysts to chemical synthesis and drug development. In this chapter, we review the discovery and function of several important heme-thiolate enzymes. Next, the characterization of intermediates in the catalytic cycle during the oxidative reactions is addressed. Finally, applications of the knowledge obtained from these mechanistic investigations on the design of new enzymatic catalysts are discussed.
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