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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.
摘要：
乳酸消旋酶是已知具有金属夹钳活性位点的第一种酶。这种酶可以将乳酸和乳酸相互转化，这对于许多微生物中细胞壁的组装很重要。这里,我们报道了乳酸消旋酶活性位点的合成模型，其特征是基于吡啶的SCS钳配体框架与镍结合。模型复合物介导醇的脱氢，与乳酸盐外消旋化相关的反应。实验和计算数据表明配体参与脱氢反应。
