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Nickel pincer model of the active site of lactate racemase involves ligand participation in hydride transfer.
Title Nickel pincer model of the active site of lactate racemase involves ligand participation in hydride transfer.
Authors Xu, T.; Wodrich, M.D.; Scopelliti, R.; Corminboeuf, C.; Hu, X.
Journal Proc Natl Acad Sci U S A
DOI 10.1073/pnas.1616038114
Abstract

Lactate racemase is the first enzyme known to possess a metal pincer active site. The enzyme interconverts d- and l-lactic acid, which is important for the assembly of cell walls in many microorganisms. Here, we report a synthetic model of the active site of lactate racemase, which features a pyridinium-based SCS pincer ligand framework bound to nickel. The model complex mediates the dehydrogenation of alcohols, a reaction relevant to lactate racemization. Experimental and computational data indicate ligand participation in the dehydrogenation reaction.