Cellular and Molecular Life Sciences CMLS

, Volume 56, Issue 7, pp 604–625

Nickel-binding proteins

Authors

  • R. K. Watt
    • 433 Babcock Dr., Madison (Wisconsin 53706, USA), Fax +1 608 262 3453, e-mail: Ludden@biochem.wisc.edu
  • P. W. Ludden
    • 433 Babcock Dr., Madison (Wisconsin 53706, USA), Fax +1 608 262 3453, e-mail: Ludden@biochem.wisc.edu

DOI: 10.1007/s000180050456

Cite this article as:
Watt, R. & Ludden, P. CMLS, Cell. Mol. Life Sci. (1999) 56: 604. doi:10.1007/s000180050456

Abstract.

Nickel enzymes are a relatively new class of metalloenzymes. The seven known nickel enzymes are urease, hydrogenase, CO-dehydrogenase, methyl-coenzyme M reductase, Ni-superoxide dismutase, glyoxalase I and cis-trans isomerase. The requirement for nickel implies the presence of a nickel-processing system, since free transition metals are harmful to the cell. A nickel-processing system involves the recognition and transport of nickel into the cell and the handling of the nickel once it enters the cell until it is inserted into the nickel enzyme. Several mechanisms for nickel transport have been identified and will be reviewed here. Accessory proteins required for the biosynthesis of the nickel active site have been identified. Accessory proteins bind the nickel when it enters the cell and are proposed to assist with the insertion of nickel into the enzyme. The function of the characterized nickel-processing proteins is described, and models for nickel insertion into the nickel enzymes are presented.

Key words. Nickel enzymes; nickel transport; nickel-processing proteins; metal chaperonin proteins; metallocluster assembly; urease; hydrogenase; CO-dehydrogenase.

Copyright information

© Birkhäuser Verlag Basel, 1999