Literature DB >> 26462450

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

Tao Xu1, Gerald Bauer1, Xile Hu2.   

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.
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

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

Mesh：

Substances：

Year:  2015        PMID： 26462450     DOI： 10.1002/cbic.201500498

Source DB:  PubMed          Journal:  Chembiochem        ISSN： 1439-4227            Impact factor:   3.164


  2 in total

1.  Nickel pincer model of the active site of lactate racemase involves ligand participation in hydride transfer.

Authors:  Tao Xu; Matthew D Wodrich; Rosario Scopelliti; Clemence Corminboeuf; Xile Hu
Journal:  Proc Natl Acad Sci U S A       Date:  2017-01-23       Impact factor: 11.205

2.  Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium carboxylation and LarE-dependent sacrificial sulfur insertion.

Authors:  Benoît Desguin; Patrice Soumillion; Pascal Hols; Robert P Hausinger
Journal:  Proc Natl Acad Sci U S A       Date:  2016-04-25       Impact factor: 11.205
  2 in total

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