The ability of copper-containing enzymes to activate dioxygen in energy metabolism and in the selective oxidation of biological substrates far surpasses the control and efficiency achieved by chemists. Methanotropic bacteria selectively and efficiently perform the methane to methanol conversion using dioxygen under benign conditions by action of the enzyme pMMO. X-ray crystallographic investigations suggest an asymmetric binuclear copper site, in which one copper is ligated by two histidine imidazole groups and another by the primary amine of an N-terminal histidine. However, the nature of the copper-dioxygen active oxidant remains poorly understood. Small-molecule synthetic complexes provide a wealth of information concerning structure-reactivity relationships, by detailing what is chemically possible if not probable. Exploration of primary amine ligation in stabilizing copper-dioxygen derived species, previously uncharacterized, will be discussed, along with their subsequent reactivity with C-H bonds. Spectroscopic, reactivity, and computational studies will rationalize the chemical importance of this structural motif to this and other copper-based oxidative enzymes.

Primary amine ligation in Cu-dioxygen activation and subsequent C-H reactivity

248th National Meeting (2014)

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