Journal
DALTON TRANSACTIONS
Volume 40, Issue 20, Pages 5604-5610Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1dt10187k
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Funding
- Polish State Committee for Scientific Research [KBN N N204 146537]
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The Hpn and HspA proteins from H. pylori are significant for nickel homeostasis and protect the cells from higher concentrations of external metal ions. Both proteins have a unique histidine-and cysteine-rich domain at the C terminus. The interactions of Ni2+, Bi3+, Zn2+ and Cd2+ ions with C-terminal Ac-CCSTSDSHHQ-NH2 and Ac-EEGCCHGHHE-NH2 fragments from Hpn and the Ac-GSCCHTGNHD-NH2 sequence from HspA were studied by potentiometry, mass spectrometry, circular dichroism and UV-Vis spectroscopy. Ac-CC-NH2 was used as a reference peptide. The studies have shown that nickel ions form planar complexes with a {2S(-), N-} binding mode. The thiol sulfurs of the -Cys-Cys- motif are also the anchoring sites for Bi3+, Zn2+ and Cd2+ ions. The studied protein fragments have the highest affinity for Bi3+ ions. The thermodynamic stability of Ni2+ is much higher then that of Zn2+.
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