Functional Models of the Nickel Pincer Nucleotide Cofactor of Lactate Racemase

Angew Chem Int Ed Engl. 2019 Nov 18;58(47):16869-16872. doi: 10.1002/anie.201910490. Epub 2019 Oct 11.

Abstract

A novel nickel pincer cofactor was recently discovered in lactate racemase. Reported here are three synthetic nickel pincer complexes that are both structural and functional models of the pincer cofactor in lactate racemase. DFT computations suggest the ipso-carbon atom of the pyridinium pincer ligands act as a hydride acceptor for lactate isomerization, whereas an organometallic pathway involving nickel-mediated β-hydride elimination is less favored.

Keywords: cofactors; enzymes; nickel; pincer ligands; reaction mechanisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Crystallography, X-Ray
  • Models, Molecular
  • Nickel / chemistry
  • Nickel / metabolism*
  • Nucleotides / chemistry
  • Nucleotides / metabolism*
  • Racemases and Epimerases / metabolism*

Substances

  • Bacterial Proteins
  • Nucleotides
  • Nickel
  • Racemases and Epimerases
  • lactate racemase