Multinuclear cuperous centers in enzymes that activate dioxygen are ligated predominantly by imidazoles from histidine residues.  Understanding the nature of intermediate species involved in their enzymatic oxidation processes informs on the design of new copper oxidation catalysts that can exploit dioxygen.  Synthetic cuperous imidazole complexes can recapitulate most of the biological intermediates from dioxygen and some even adventure beyond into the Cu(III) oxidation state realm, albeit at low temperatures. However, no copper enzyme is known to stabilize a copper site in the Cu(III) oxidation state to date. The role of imidazole in stabilizing Cu(III) species will be the focus of the presentation.<br/>

Cu(III) with imidazole ligation: Biologic relevance?

254th National Meeting (2017)

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