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Article: Thermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn

TitleThermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpn
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2006, v. 128 n. 35, p. 11330-11331 How to Cite?
AbstractThe 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+ ≈ 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. Copyright © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/68081
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGe, Ren_HK
dc.contributor.authorZhang, Yen_HK
dc.contributor.authorSun, Xen_HK
dc.contributor.authorWatt, RMen_HK
dc.contributor.authorHe, QYen_HK
dc.contributor.authorHuang, JDen_HK
dc.contributor.authorWilcox, DEen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:01:09Z-
dc.date.available2010-09-06T06:01:09Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2006, v. 128 n. 35, p. 11330-11331en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68081-
dc.description.abstractThe 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+ ≈ 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. Copyright © 2006 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshBacterial Proteins - chemistry - geneticsen_HK
dc.subject.meshBinding, Competitiveen_HK
dc.subject.meshBismuth - chemistry - pharmacologyen_HK
dc.subject.meshCopper Sulfate - chemistry - pharmacologyen_HK
dc.subject.meshEdetic Acid - chemistryen_HK
dc.subject.meshEscherichia coli - drug effects - genetics - growth & developmenten_HK
dc.subject.meshHydrogen-Ion Concentrationen_HK
dc.subject.meshKineticsen_HK
dc.subject.meshMetals - chemistry - pharmacologyen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNickel - chemistry - pharmacologyen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProteins - chemistry - geneticsen_HK
dc.subject.meshRanitidine - analogs & derivatives - chemistry - pharmacologyen_HK
dc.subject.meshThermodynamicsen_HK
dc.subject.meshZinc Sulfate - chemistry - pharmacologyen_HK
dc.titleThermodynamic and kinetic aspects of metal binding to the histidine-rich protein, Hpnen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0002-7863&volume=128&spage=11330&epage=11331&date=2006&atitle=Thermodynamic+and+kinetic+aspects+of+metal+binding+to+the+histidine-rich+protein,+Hpnen_HK
dc.identifier.emailWatt, RM:rmwatt@hku.hken_HK
dc.identifier.emailHuang, JD:jdhuang@hkucc.hku.hken_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authorityWatt, RM=rp00043en_HK
dc.identifier.authorityHuang, JD=rp00451en_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/ja062589ten_HK
dc.identifier.pmid16939237en_HK
dc.identifier.scopuseid_2-s2.0-33748372299en_HK
dc.identifier.hkuros121159en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33748372299&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume128en_HK
dc.identifier.issue35en_HK
dc.identifier.spage11330en_HK
dc.identifier.epage11331en_HK
dc.identifier.isiWOS:000240116300007-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridZhang, Y=35075542200en_HK
dc.identifier.scopusauthoridSun, X=8906547400en_HK
dc.identifier.scopusauthoridWatt, RM=7102907536en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.scopusauthoridHuang, JD=8108660600en_HK
dc.identifier.scopusauthoridWilcox, DE=7102818229en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.citeulike3814271-

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