Liver alcohol dehydrogenase (LADH) is a zinc metalloenzyme that catalyzes the oxidation of alcohols to aldehydes and ketones, and the reduction of a ketone or an aldehyde to an alcohol. The resting enzyme has a zinc(II) metal center which is pseudo-tetrahedrally ligated with one N-histidine side chain, two S-cysteine side chains, and one water molecule. Our work involves the syntheses, spectroscopic and electrochemical characterizations, quantum chemical calculations, and activity screening of potential functional models of the zinc active site in LADH. We model the zinc active site using a family of tridentate pincer ligands coordinating S,N,S or N,N,N donor atoms. DFT calculations are performed to better understand the geometries about the zinc center. A detailed description of the syntheses and characterization of the ligand precursors and model complexes will be presented along with reactivity findings and DFT calculations.

Syntheses, characterization, DFT calculations and activity of tridentate SNS or NNN zinc pincer complexes based on bis-imidazole or bis-triazole precursors

244th National Meeting (2012)

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