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Abstract
Most biological oxidations of exogenous compounds, such as drugs and endogenous compounds, especially when the hydroxylation of an inert C-H bond is involved, are catalyzed by cytochrome P-450-dependent monooxygenases. These enzymes have the unique ability to transfer an oxygen atom from oxygen atom donors including O2 into almost any organic substrates including alkanes in a highly selective manner. Based on the knowledge of the mechanisms of substrate oxidation by these cytochromes, chemical model systems using metalloporphyrin catalysts have been built. In particular, a very efficient system for hydrocarbon oxidation by H2O2 in mild conditions is described. It is also shown that Fe- and Mn-porphyrins catalyze the transfer of the NR nitrene moiety of PhI=NR compounds into hydrocarbons leading to direct aziridination of alkenes and amidation of alkanes with high yields.
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