A Novel Nickel Pincer Complex in the Active Site of Lactate Racemase

Tao Xu; Gerald Bauer; Xile Hu

doi:10.1002/cbic.201500498

A Novel Nickel Pincer Complex in the Active Site of Lactate Racemase

Chembiochem. 2016 Jan;17(1):31-2. doi: 10.1002/cbic.201500498. Epub 2015 Nov 4.

Authors

Tao Xu¹, Gerald Bauer¹, Xile Hu²

Affiliations

¹ Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), ISCI-LSCI, BCH 3305, 1015, Lausanne, Switzerland.
² Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), ISCI-LSCI, BCH 3305, 1015, Lausanne, Switzerland. xile.hu@epfl.ch.

PMID: 26462450
DOI: 10.1002/cbic.201500498

Abstract

Put through the pincer: A recent study revealed the structure of the Ni-containing active site of lactate racemase. The Ni is coordinated by a SCS pincer ligand derived from a nicotinic acid mononucleotide.

Keywords: hydride transfer; lactate racemase; nickel; pincer complexes.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Bacterial Proteins / chemistry*
Lactic Acid / biosynthesis*
Lactobacillus plantarum / enzymology*
Metalloproteins / chemistry*
Niacin / chemistry*
Nickel / chemistry*
Racemases and Epimerases / chemistry*

Substances

Bacterial Proteins
Metalloproteins
Niacin
Lactic Acid
Nickel
Racemases and Epimerases