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Article: Binding of Ni2+ to a histidine- and glutamine-rich protein, Hpn-like

TitleBinding of Ni2+ to a histidine- and glutamine-rich protein, Hpn-like
Authors
Issue Date2008
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm
Citation
Journal Of Biological Inorganic Chemistry, 2008, v. 13 n. 7, p. 1121-1131 How to Cite?
AbstractHpn-like (Hpnl) protein, encoded by the hpnl gene in Helicobacter pylori and featuring a histidine-rich and two glutamine-rich motifs, can render nickel tolerance to H. pylori when the external nickel level reaches toxic limits. We found that the recombinant Hpnl exists as an oligomer in the native state and binds to two molar equivalents of nickel ions per monomer with a dissociation constant of 3.8 μM. Nickel could be released from Hpnl either at acidic pH (pH1/2 4.6) or in the presence of chelate ligands, such as EDTA (t 1/2 = 220, 355, and 716 min at pH 6.0, 7.0, and 7.5, respectively). Our combined spectroscopic data show that nickel ion coordinates to a nitrogen of a histidine residue possibly with a coordination number of four (square-planar geometry) or five. The growth of Escherichia coli cells with or without the hpnl gene implied a protective role of Hpnl under higher concentrations of external nickel ions. Hpnl may serve a role in binding/storage or detoxification of excess nickel ions. © 2008 SBIC.
Persistent Identifierhttp://hdl.handle.net/10722/168324
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZeng, YBen_US
dc.contributor.authorZhang, DMen_US
dc.contributor.authorLi, Hen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2012-10-08T03:17:33Z-
dc.date.available2012-10-08T03:17:33Z-
dc.date.issued2008en_US
dc.identifier.citationJournal Of Biological Inorganic Chemistry, 2008, v. 13 n. 7, p. 1121-1131en_US
dc.identifier.issn0949-8257en_US
dc.identifier.urihttp://hdl.handle.net/10722/168324-
dc.description.abstractHpn-like (Hpnl) protein, encoded by the hpnl gene in Helicobacter pylori and featuring a histidine-rich and two glutamine-rich motifs, can render nickel tolerance to H. pylori when the external nickel level reaches toxic limits. We found that the recombinant Hpnl exists as an oligomer in the native state and binds to two molar equivalents of nickel ions per monomer with a dissociation constant of 3.8 μM. Nickel could be released from Hpnl either at acidic pH (pH1/2 4.6) or in the presence of chelate ligands, such as EDTA (t 1/2 = 220, 355, and 716 min at pH 6.0, 7.0, and 7.5, respectively). Our combined spectroscopic data show that nickel ion coordinates to a nitrogen of a histidine residue possibly with a coordination number of four (square-planar geometry) or five. The growth of Escherichia coli cells with or without the hpnl gene implied a protective role of Hpnl under higher concentrations of external nickel ions. Hpnl may serve a role in binding/storage or detoxification of excess nickel ions. © 2008 SBIC.en_US
dc.languageengen_US
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htmen_US
dc.relation.ispartofJournal of Biological Inorganic Chemistryen_US
dc.subject.meshAmino Acid Motifsen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshApoproteins - Chemistry - Metabolismen_US
dc.subject.meshBacterial Proteins - Chemistry - Metabolismen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCell Proliferation - Drug Effectsen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEscherichia Coli - Cytology - Drug Effects - Geneticsen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshGlutamineen_US
dc.subject.meshHelicobacter Pylori - Metabolismen_US
dc.subject.meshHistidineen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNickel - Metabolism - Pharmacologyen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Multimerizationen_US
dc.subject.meshProtein Structure, Quaternaryen_US
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleBinding of Ni2+ to a histidine- and glutamine-rich protein, Hpn-likeen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s00775-008-0397-0en_US
dc.identifier.pmid18563455-
dc.identifier.scopuseid_2-s2.0-51849097276en_US
dc.identifier.hkuros152162-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-51849097276&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume13en_US
dc.identifier.issue7en_US
dc.identifier.spage1121en_US
dc.identifier.epage1131en_US
dc.identifier.isiWOS:000259248900008-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridZeng, YB=7402981405en_US
dc.identifier.scopusauthoridZhang, DM=8657548700en_US
dc.identifier.scopusauthoridLi, H=14023043100en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.citeulike3814176-

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