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The structure and function of nickel sites in metalloproteins

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Less Common Metals in Proteins and Nucleic Acid Probes

Part of the book series: Structure and Bonding ((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.

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Authors and Affiliations

  1. Department of Chemistry and Program in Molecular and Cellular Biology, University of Massachusetts, 01003-4510, Amherst, MA, USA

    Michael J. Maroney, Gerard Davidson, Christian B. Allan & James Figlar

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  1. Michael J. Maroney
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  2. Gerard Davidson
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Maroney, M.J., Davidson, G., Allan, C.B., Figlar, J. (1998). The structure and function of nickel sites in metalloproteins. In: Less Common Metals in Proteins and Nucleic Acid Probes. Structure and Bonding, vol 92. Springer, Berlin, Heidelberg . https://doi.org/10.1007/BFb0081077

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