The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions
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 th...
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Veröffentlicht in: | Dalton transactions : an international journal of inorganic chemistry 2013-05, Vol.42 (17), p.6012-6020 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 1477-9226 1477-9234 |
DOI: | 10.1039/c2dt32195e |