Thermodynamic and Kinetic Aspects of Metal Binding to the Histidine-rich Protein, Hpn
Journal of the American Chemical Society2006Vol. 128(35), pp. 11330–11331
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Ruiguang Ge, Yi Zhang, Xuesong Sun, Rory M. Watt, Qing‐Yu He, Jian‐Dong Huang, Dean E. Wilcox, Hongzhe Sun
Abstract
The histidine-rich protein, Hpn, binds to essential metals Ni2+, Cu2+, Zn2+ and a therapeutic metal Bi3+ with the in vitro affinities in the order of Cu2+ > Ni2+ > Bi3+ > Zn2+. In contrast, the in vivo (in E. coli) protection by the protein is in the order of Ni2+ > Bi3+ > Cu2+ approximately Zn2+. The release of Ni2+ from the protein follows a two-step process consisting of a rapidly established equilibrium and subsequently a rate-determining step (dissociation of Hpn-Ni...EDTA to Ni-EDTA). Our work suggests the nickel storage and homeostasis in H. pylori as the primary role of Hpn.
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