Abstract
Selective functionalization of unactivated C–H bonds is an extremely important industrial process. A wide variety of metalloenzymes perform the challenging oxidative C–H bond activation reactions in biology by activating dioxygen and hydrogen peroxide at dinuclear active sites containing cheap and abundant transition metals like iron, copper and manganese. Metal-dioxygen or high-valent metal-oxo complexes act as reactive intermediates in many of these processes. They are often very reactive and difficult to isolate. Accordingly, the synthesis and spectroscopic characterization and detailed reactivity studies of bioinspired model compounds are often undertaken in order to obtain vital insights into the mechanism of the enzymatic reactions. In this review, we summarize the information obtained to date in biological and bioinspired model systems regarding the mechanism of oxidative transformations taking place at the dimetallic centers containing exclusively non-heme iron and manganese centers.
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