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 in particulate methane monooxygenase and a variety of monocopper enzymes. 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, and have studied a number of intriguing species featuring Cu(III) centers. Recent progress toward the characterization of the structures and properties of such species will be described, with particular focus on their reactions with C-H and O-H bonds.

<b>Award Address</b> (ACS Award for Distinguished Service in the Advancement of Inorganic Chemistry sponsored by Strem Chemicals, Inc.). Copper-Oxygen complexes relevant to enzyme intermediates

253rd National Meeting (2017)

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Award Address (ACS Award for Distinguished Service in the Advancement of Inorganic Chemistry sponsored by Strem Chemicals, Inc.). Copper-Oxygen complexes relevant to enzyme intermediates