File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Lipoprotein MtsA of MtsABC in Streptococcus pyogenes primarily binds ferrous ion with bicarbonate as a synergistic anion

TitleLipoprotein MtsA of MtsABC in Streptococcus pyogenes primarily binds ferrous ion with bicarbonate as a synergistic anion
Authors
KeywordsBicarbonate
Ferrous ion
Metal binding
MtsA
Streptococcus pyogenes
Issue Date2008
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2008, v. 582 n. 9, p. 1351-1354 How to Cite?
AbstractLipoprotein MtsA is a critical component of MtsABC responsible for iron binding and transport in the Gram-positive bacterium Streptococcus pyogenes. The present collective experimental data establish that Fe2+ is the primary binding ion for MtsA under optimal physiologically relevant conditions. The binding affinities of MtsA to metal ions are Fe2+ > Fe3+ >Cu2+ > Mn2+ > Zn2+. We report for the first time that bicarbonate is required as a synergistic anion for stable ferrous binding to MtsA, similar to the iron binding in human transferrin. This work provides valuable information, which helps to understand iron metabolism in bacteria, and creates a basis for developing strategies to suppress bacterial infection. © 2008 Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/69400
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Xen_HK
dc.contributor.authorGe, Ren_HK
dc.contributor.authorChiu, JFen_HK
dc.contributor.authorSun, Hen_HK
dc.contributor.authorHe, QYen_HK
dc.date.accessioned2010-09-06T06:13:19Z-
dc.date.available2010-09-06T06:13:19Z-
dc.date.issued2008en_HK
dc.identifier.citationFebs Letters, 2008, v. 582 n. 9, p. 1351-1354en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69400-
dc.description.abstractLipoprotein MtsA is a critical component of MtsABC responsible for iron binding and transport in the Gram-positive bacterium Streptococcus pyogenes. The present collective experimental data establish that Fe2+ is the primary binding ion for MtsA under optimal physiologically relevant conditions. The binding affinities of MtsA to metal ions are Fe2+ > Fe3+ >Cu2+ > Mn2+ > Zn2+. We report for the first time that bicarbonate is required as a synergistic anion for stable ferrous binding to MtsA, similar to the iron binding in human transferrin. This work provides valuable information, which helps to understand iron metabolism in bacteria, and creates a basis for developing strategies to suppress bacterial infection. © 2008 Federation of European Biochemical Societies.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsF E B S Letters. Copyright © Elsevier BV.en_HK
dc.subjectBicarbonateen_HK
dc.subjectFerrous ionen_HK
dc.subjectMetal bindingen_HK
dc.subjectMtsAen_HK
dc.subjectStreptococcus pyogenesen_HK
dc.titleLipoprotein MtsA of MtsABC in Streptococcus pyogenes primarily binds ferrous ion with bicarbonate as a synergistic anionen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-5793&volume=582&spage=1351&epage=1354&date=2008&atitle=Lipoprotein+MtsA+of+MtsABC+in+Streptococcus+pyogenes+primarily+binds+ferrous+ion+with+bicarbonate+as+a+synergistic+anionen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.febslet.2008.03.020en_HK
dc.identifier.pmid18364240-
dc.identifier.scopuseid_2-s2.0-41449096957en_HK
dc.identifier.hkuros141585en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-41449096957&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume582en_HK
dc.identifier.issue9en_HK
dc.identifier.spage1351en_HK
dc.identifier.epage1354en_HK
dc.identifier.isiWOS:000258004500012-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridSun, X=8906547400en_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridChiu, JF=7201501692en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats