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The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
Autorzy
Rok wydania
2013
Czasopismo
Numer woluminu
42
Strony
6012-6020
DOI
10.1039/c2dt32195e
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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.
Adres publiczny
http://dx.doi.org/10.1039/c2dt32195e