Methanol dehydrogenase is a ubiquitous enzyme in bacterial methane metabolism. Recently, a lanthanide (Ln) cation was discovered within the active site of an XoxF-type dehydrogenase, which has prompted a new research area of lanthanide biochemistry and biology. We reported the first synthetic, functional model of a Ln-dependent dehydrogenase that was capable of both stoichiometric and catalytic dehydrogenation of 4-methylbenzyl alcohol. Density functional theory (DFT) calculations, where nitrates were used as k<sup>2</sup>-bound anions, suggested a prevailing hydride transfer mechanism for this reaction. On the other hand, efforts toward use of more biologically relevant bases, such as acetate or deprotonated amino acids, could further probe this mechanism. We found that DFT calculations using the more basic acetate anions, compared to nitrate, indicate changes to the relative energies of the transition states involved in these two competing mechanisms. Findings from this theoretical study will be discussed.

Theoretical studies of a lanthanide-dependent methanol dehydrogenase model system

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.