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Chem Commun (Camb). 2014 Feb 14;50(13):1611-4. doi: 10.1039/c3cc47644h.

Functional disruption of HypB, a GTPase of Helicobacter pylori, by bismuth.

Author information

1
Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, P. R. China. hsun@hku.hk.

Abstract

Bismuth (Bi(3+)) binds equal molar amounts of HypB from Helicobacter pylori at the conserved metal site with a dissociation constant of 0.94 (±0.25) × 10(-17) μM, and concomitantly induces the protein dimerization similarly to Ni(2+). Excess Bi(3+) causes HypB further oligomerization, leading to HypB GTPase dysfunction. The results extend our understanding on the inhibitory mechanism of bismuth drugs against the pathogen.

PMID:
24389922
DOI:
10.1039/c3cc47644h
[Indexed for MEDLINE]

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