Related ArticlesThe zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
Dalton Trans. 2013 Jan 21;
Authors: Rowinska-Zyrek M, Potocki S, Witkowska D, Valensin D, Kozlowski H
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.
PMID: 23338727 [PubMed - as supplied by publisher]
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Stepan B. Lesnichin, Ilya G. Shenderovich, Titin Muljati, David Silverman and Hans-Heinrich Limbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203478j/aop/images/medium/ja-2011-03478j_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203478j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/pgOKoZytT3U
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The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
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