Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 140, Issue 4, Pages 1223-1226Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b12318
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Funding
- U.S. NSF [CHE-1608925, OCI-1053575]
- University of Pennsylvania
- Camille and Henry Dreyfus Postdoctoral Program in Environmental Chemistry
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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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