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Related Experiment Videos

Nickel(II) binding to Cap43 protein fragments.

M A Zoroddu1, M Peana, T Kowalik-Jankowska

  • 1Department of Chemistry and Pharmacy Faculty, University of Sassari, Via Vienna 2, 07100 Sassari, Italy. zoroddu@uniss.it

Journal of Inorganic Biochemistry
|May 20, 2004
PubMed
Summary

Cap43 protein contains a novel metal-binding site in its C-terminus. This site, featuring a repeated histidine motif, effectively binds nickel ions, forming stable complexes at physiological and higher pH levels.

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Area of Science:

  • Biochemistry
  • Metalloprotein studies
  • Protein structure and function

Background:

  • Cap43 protein is induced by nickel compounds in human cells.
  • A novel mono-histidinic motif, repeated thrice in the C-terminus, was identified.
  • This motif is a potential nickel-binding site.

Purpose of the Study:

  • To investigate the Ni(II) binding capabilities of Cap43 protein's C-terminal fragments.
  • To characterize the metal-ligand complexes formed.
  • To determine the coordination environment of Ni(II) ions.

Main Methods:

  • Synthesis and analysis of two peptides (20- and 30-amino acid) representing the C-terminal motif.
  • Combined pH-metric and spectroscopic (UV-visible, CD, NMR) studies.

Related Experiment Videos

  • Analysis of Ni(II) binding stoichiometry and complex formation.

    • Main Results:

    • Both peptides bind Ni(II) ions, with the 30-amino acid peptide binding up to three metal ions.
    • Complexes formed include Ni(2)L (peptide 1) and NiL, Ni(2)L, Ni(3)L (peptide 2) at physiological pH.
    • Coordination involves histidine imidazole nitrogen atoms, forming octahedral complexes at pH 8-9 and planar 4N complexes above pH 9.

    Conclusions:

    • The C-terminal domain of Cap43 protein possesses a significant Ni(II) binding site.
    • The identified histidine-rich motif is crucial for nickel coordination.
    • This finding contributes to understanding metalloprotein interactions and potential roles in nickel homeostasis or toxicity.