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Our current interests focus on stabilizing species formed in the reaction of dioxygen with Cu(I) complexes formed with biologically relevant imidazole or histamine ligation. Many multi-copper enzymes ligated in this manner are capable of impressive hydroxylation reactions, including oxidative depolymerization of cellulose, methane oxidation, and energy-efficient reduction of dioxygen to water. Oxygenation of such complexes at extreme solution temperatures (-125°C) yield transient Cu(III) containing complexes. As Cu(III) is currently uncharacterized in any biological enzyme, developing connections between the synthetic and biological realms is a major focus.
In redox active biological metal sites, the ligation environment is coupled tightly to the functional chemistry. Yet, the metal sites are also site-isolated, creating species that may only have a transient existence in a homogeneous solution. Site isolation of synthetic complexes can be achieved synthetically by supporting the metal complex on a solid matrix. Movement of these complexes into silica based materials or onto electroactive carbon electrodes represent a new direction for the group in the development of bio-inspired metal-based catalysts.
In redox active biological metal sites, the ligation environment is coupled tightly to the functional chemistry. Yet, the metal sites are also site-isolated, creating species that may only have a transient existence in a homogeneous solution. Site isolation of synthetic complexes can be achieved synthetically by supporting the metal complex on a solid matrix. Movement of these complexes into silica based materials or onto electroactive carbon electrodes represent a new direction for the group in the development of bio-inspired metal-based catalysts.
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FARADAY DISCUSSIONSno. 0 (2022): 129-142
Samuel J. Fretz, Christopher T. Lyons,Ella Levin,Christopher E. D. Chidsey,Anders E. C. Palmqvist,T. Daniel P. Stack
Inorganica chimica acta (2017): 151-158
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