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Issue 17, 2013
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The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions

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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-NH2). There are at least three hypotheses on the binding mode of this ion. In this paper, we try to understand how Zn2+ binds to this fragment and why Ni2+, 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.

Graphical abstract: The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions

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Publication details

The article was received on 21 Sep 2012, accepted on 11 Dec 2012 and first published on 11 Dec 2012


Article type: Paper
DOI: 10.1039/C2DT32195E
Citation: Dalton Trans., 2013,42, 6012-6020
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    The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions

    M. Rowinska-Zyrek, S. Potocki, D. Witkowska, D. Valensin and H. Kozlowski, Dalton Trans., 2013, 42, 6012
    DOI: 10.1039/C2DT32195E

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