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Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase
Published on: March 19, 2020
Functional Synthetic Model for the Lanthanide-Dependent Quinoid Alcohol Dehydrogenase Active Site
Alex McSkimming1, Thibault Cheisson1, Patrick J Carroll1
1P. Roy and Diana T. Vagelos Laboratories, Department of Chemistry, University of Pennsylvania , 231 S 34th Street, Philadelphia, Pennsylvania 19104, United States.
Abstract:
The oxidation of methanol by dehydrogenase enzymes is an essential part of the bacterial methane metabolism cycle. The recent discovery of a lanthanide (Ln) cation in the active site of the XoxF dehydrogenase represents the only example of a rare-earth element in a physiological role. Herein, we report the first synthetic, functional model of Ln-dependent dehydrogenase and its stoichiometric and catalytic dehydrogenation of a benzyl alcohol. Density functional theory calculations implicate a hydride transfer mechanism for these reactions.
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