Abstract

High valent iron-oxo species are often invoked as the key oxidizing agents in the catalytic cycles of oxygen activating nonheme iron enzymes, and three of these intermediates have in fact been characterized. To gain further insight into such species, a number of biomimetic complexes have been designed and investigated as functional models for these enzymes. Progress since 2000 is summarized in this review. Many of the model complexes discussed in this review carry out oxidative transformations of relevance to the enzymatic reactions; however, the participation of a high-valent iron-oxo species (Fe IV O or Fe V O) can only be inferred. Arguments in support of a metal-based oxidant (rather than an oxygen radical species) usually hinge on the high conversion for the transformation and the nature of the reaction products, as well as the incorporation of label into these products from H 2 18O or related species. Within this time period, the first bona fide nonheme Fe IV O complexes have been generated and identified spectroscopically, three of which are crystallographically characterized. Taken together, these studies emphasize the important role the supporting polydentate ligand plays in eliciting the desired high-valent iron-oxo chemistry.

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