Characterization of copper intermediates in enzymes and other catalysts that attack strong C-H bonds is important for unraveling oxidation catalysis mechanisms and, ultimately, designing new, more efficient catalytic systems. New insights into the nature of such intermediates may be obtained through the design, synthesis, and characterization of copper-oxygen complexes. Particular impetus for such studies comes from provocative proposals of novel structures for the oxidizing species a variety of monocopper enzymes, of which lytic polysaccharide monooxygenase (LPMO) is of particular note due to its novel structure and its utility in biotechnology. In work aimed at synthesizing molecules with such cores, we have turned to the use of strongly electron donating carboxamide ligands designed to stabilize copper in high oxidation states. In this lecture, we focus on comparing the reactivity of complexes with [CuO2]+ and [CuOH]2+ cores having the same supporting ligand with C-H and O-H bonds. Intriguing differences in their mechanisms of proton-coupled electron-transfer will be discussed.

Proton-coupled electron transfer mechanisms in copper-oxygen chemistry

2019 Fall National Meeting

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