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. |