Issue 17, 2013
From the journal:

Dalton Transactions

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

Magdalena Rowinska-Zyrek,a   Slawomir Potocki,a   Danuta Witkowska,a   Daniela Valensinb  and  Henryk Kozlowski*a  

* Corresponding authors

a Department of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland
E-mail: henryk.kozlowski@chem.uni.wroc.pl

b Department of Chemistry, University of Siena, via Aldo Moro, 53100 Siena, Italy

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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Article information

DOI
https://doi.org/10.1039/C2DT32195E
Article type
Paper
Submitted
21 Sep 2012
Accepted
11 Dec 2012
First published
11 Dec 2012

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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