Xu Tao, Wodrich Matthew D, Scopelliti Rosario, Corminboeuf Clemence, Hu Xile
Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland.
Laboratory for Computational Molecular Design, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland.
Proc Natl Acad Sci U S A. 2017 Feb 7;114(6):1242-1245. doi: 10.1073/pnas.1616038114. Epub 2017 Jan 23.
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.
乳酸消旋酶是已知的第一种具有金属钳形活性位点的酶。该酶可使d-乳酸和l-乳酸相互转化，这对许多微生物细胞壁的组装很重要。在此，我们报道了一种乳酸消旋酶活性位点的合成模型，其特征是一个与镍结合的基于吡啶鎓的SCS钳形配体框架。该模型配合物介导醇的脱氢反应，这是一个与乳酸消旋化相关的反应。实验和计算数据表明配体参与了脱氢反应。
