Multielectron processes performed by metalloenzymes are ubiquitous in nature. Of the many non-heme metalloenzymes, several have redox activity that enable their function. The superoxide dismutase (SOD) family of enzymes, for example, regulates the reactive oxygen species superoxide (O2●-) using its redox active metal center. Synthetic models of the Cu,Zn-SOD and NiSOD have been made in attempts to elucidate the mechanism of dismutation from O2●- to O2. In SOD, the active site oxidizes O2●- which results in the one-electron reduction of CuII, producing CuI. Continued research on active sites of metalloenzymes could break down current barriers in performing organic transformations. Toward this goal, a new redox active [NNN]-type ligand has been designed to enable first-row transition metals to overcome their limitation of performing single-electron chemistry. NiII, CuII, and ZnII complexes have been prepared, which have been studied via UV/vis, EPR, and NMR spectroscopies, elemental analysis and cyclic voltammetry. This presentation will detail the molecular structures, physical properties, and reactivity of these complexes to demonstrate the role of the redox active ligand in facilitating multielectron processes.

Ligand imparts redox active character in earth-abundant metal complexes for multielectron processes

255th National Meeting (2018)

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