期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 6, 页码 1242-1245出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1616038114
关键词
biomimetic chemistry; lactate racemase; nickel; pincer ligands; hydride transfer
资金
- Swiss National Science Foundation [200020_152850/1]
- Ecole Polytechnique Federale de Lausanne
- Swiss National Science Foundation (SNF) [200020_152850] Funding Source: Swiss National Science Foundation (SNF)
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.
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