Functional Synthetic Model for the Lanthanide-Dependent Quinoid Alcohol Dehydrogenase Active Site.

The oxidation of methanol by dehydrogen-ase 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 re...

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Bibliographic Details
Published in:	Journal of the American Chemical Society Vol. 140; no. 4; pp. 1223 - 1227
Main Authors:	McSkimming, Alex, Cheisson, Thibault, Carroll, Patrick J., Schelter, Eric J.
Format:	Article
Published:	American Chemical Society 1/31/2018
Subjects:	Quinoidine Catalytic dehydrogenation Density functional theory Alcohol dehydrogenase Oxidation of methanol
Online Access:	View this record in EBSCOhost

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Summary:	The oxidation of methanol by dehydrogen-ase 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.