This presentation will focus on our recent results concerning the stabilization, reactivity, and mechanism of high-valent metal-oxo species. High-valent Mn-oxo and Fe-oxo species play an important role in many biological systems, including a number of heme- and non-heme enzymes. These enzymes catalyze key oxidation reactions in numerous biological pathways, and it is the high-valent metal-oxo species that is believed to function as the critical oxidant. Our lab has designed and constructed the corrolazine ligand platform to stabilize high-valent metal-oxo species, and it is based on the tetrapyrrolic framework common to the heme enzyme cofactor. Reactions that are of fundamental importance for both biology (e.g. heme enzymes) and for synthetic catalysts involve oxygen-atom-transfer (OAT) and proton-coupled electron-transfer (PCET), and we will present our latest findings on these processes involving high-valent metal-oxo model systems with the corrolazine platform.

Ligand design and high-valent metal-oxo reactivity in porphyrinoid systems

244th National Meeting (2012)

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