Nickel pincer model of the active site of lactate racemase involves ligand participation in hydride transfer.
Ontology highlight
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.
SUBMITTER: Xu T
PROVIDER: S-EPMC5307482 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
ACCESS DATA