Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6253
Title: The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions
Authors: Rowinska Zyrek, Magdalena
Potocki, Slawomir
Witkowska, Danuta
Valensin, Daniela 
Kozlowski, Henryk
Keywords: Amino Acid Motifs; Bacterial Proteins; Carrier Proteins; Circular Dichroism; Coordination Complexes; Helicobacter pylori; Ions; Molecular Sequence Data; Nickel; Protein Binding; Sequence Alignment; Thermodynamics; Zinc
Issue Date: 2013
Project: None 
Journal: DALTON TRANSACTIONS
Abstract: 
HypA, a nickel accessory protein from H. pylori, binds a zinc ion in it's structural site, a loop with two conserved CXXC motifs (Ac-ELECKDCSHVFKPNALDYGVCEKCHS-NH(2)). There are at least three hypotheses on the binding mode of this ion. In this paper, we try to understand how Zn(2+) binds to this fragment and why Ni(2+), a metal with quite a high affinity towards thiolic sites, doesn't compete with zinc in the binding to this motif. Potentiometric titrations, mass spectrometry, NMR, UV-Vis and CD spectroscopy help us to compare the coordination modes in both metal complexes and discuss their thermodynamic stabilities.
Description: 
63621
URI: http://hdl.handle.net/20.500.12779/6253
ISSN: 1477-9226
DOI: 10.1039/c2dt32195e
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