Acireductone dioxygenase (ARD) is a metalloenzyme that has been of recent interest due to its dual chemistry based solely on the identity of the metal ion at its active site. Depending on whether nickel or iron is bound, the enzymatic products vary. In order to help explain why this dual chemistry occurs, a new model of the active site of Ni-ARD was synthesized and characterized, [NiII(OPhNO2(6-H-DPEN)(H2O))]+. Oxidative reactivity studies involving model substrates were performed and monitored via 1H-NMR. Preliminary evidence of biomimetic type activity mediated by this model system, including the possible activation of ethanol, will be discussed.

Evidence of biomimetic type reactivity for a model system of nickel acireductone dioxygenase (Ni-ARD)

2019 Spring National Meeting

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