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The structure and function of nickel sites in metalloproteins

  • Michael J. MaroneyEmail author
  • Gerard Davidson
  • Christian B. Allan
  • James Figlar
Chapter
Part of the Structure and Bonding book series (STRUCTURE, volume 92)

Abstract

The known Ni enzymes now include ureases, hydrogenases, carbon monoxide dehydrogenases, acetyl coenzyme A synthases, methyl coenzyme M reductases and superoxide dismutases. These enzymes employ Ni in roles varying from Lewis acid sites to involvement in redox catalysis. In addition, mechanisms involving proteins that specifically bind Ni have evolved for the acquisition, transport, and incorporation of Ni. Various biophysical techniques have been used to elucidate aspects of the structure and function of the Ni sites in these enzymes and proteins. This pursuit has been greatly advanced since 1995 by the availability of crystal structures of Klebsiella aerogenese urease, various hydrogenases, and two states of methyl coenzyme M reductase from Methanobacterium thermoautotrophicum. The knowledge of the structure and function of the various Ni proteins and enzymes is briefly overviewed. Proposals for catalytic mechanisms based on these studies and on model chemistry are presented.

Keywords

Urease hydrogenase carbon monoxide dehydrogenase acetyl coenzyme A synthase methyl coenzyme M reductase superoxide dismutase cofactor F430 

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Copyright information

© Springer Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • Michael J. Maroney
    • 1
    Email author
  • Gerard Davidson
    • 1
  • Christian B. Allan
    • 1
  • James Figlar
    • 1
  1. 1.Department of Chemistry and Program in Molecular and Cellular BiologyUniversity of MassachusettsAmherstUSA

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