Acireductone dioxygenase (ARD) is a naturally occurring metalloenzyme found in the methionine salvage pathway in plants and bacteria that is capable of catalyzing two distinct oxidative reactions, depending on the metal cofactor that is present at the active site. Ni-ARD is of particular interest due to this enzyme’s ability to generate carbon monoxide, a known antiapoptotic and signaling molecule, as a product of substrate turnover. For this research, a new biomimetic model was synthesized and characterized as a derivative of the first structural model for the resting state active site of Ni-ARD. The coordination environment of this new model system was used to probe how differences in the ligand donors affect reactivity.<i> In-situ</i> NMR studies with model substrate compounds were performed to test the biomimetic activity of this model system.

Probing the effects of the ligand environment on the biomimetic reactivity of a nickel acireductone dioxygenase model system

2019 Spring National Meeting

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