Document Detail


The zinc-binding fragment of HypA from Helicobacter pylori: a tempting site also for nickel ions.
MedLine Citation:
PMID:  23338727     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Magdalena Rowinska-Zyrek; Slawomir Potocki; Danuta Witkowska; Daniela Valensin; Henryk Kozlowski
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-21
Journal Detail:
Title:  Dalton transactions (Cambridge, England : 2003)     Volume:  -     ISSN:  1477-9234     ISO Abbreviation:  Dalton Trans     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101176026     Medline TA:  Dalton Trans     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland. henryk.kozlowski@chem.uni.wroc.pl.
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