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Article: The low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
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TitleThe low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
 
AuthorsSun, X1
Sun, H1
Ge, R1
Richter, M2
Woodworth, RC2
Mason, AB2
He, QY1
 
KeywordsAnion binding
BHK, baby-hamster kidney cells
Heteronuclear single-quantum coherence nuclear magnetic resonance
hTF, human serum transferrin
hTF/2N, recombinant N-lobe of human transferrin comprising residues 1-337
pK a
Transferrin
Tyrosine
 
Issue Date2004
 
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
 
CitationFebs Letters, 2004, v. 573 n. 1-3, p. 181-185 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.febslet.2004.07.076
 
Abstract2D NMR-pH titrations were used to determine pKa values for four conserved tyrosine residues, Tyr45, Tyr85, Tyr96 and Tyr188, in human transferrin. The low pKa of Tyr188 is due to the fact that the iron-binding ligand interacts with Lys206 in open-form and with Lys296 in the closed-form of the protein. Our current results also confirm the anion binding of sulfate and arsenate to transferrin and further suggest that Tyr188 is the actual binding site for the anions in solution. These data indicate that Tyr188 is a critical residue not only for iron binding but also for chelator binding and iron release in transferrin. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
 
ISSN0014-5793
2013 Impact Factor: 3.341
2013 SCImago Journal Rankings: 2.342
 
DOIhttp://dx.doi.org/10.1016/j.febslet.2004.07.076
 
ISI Accession Number IDWOS:000223697200031
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSun, X
 
dc.contributor.authorSun, H
 
dc.contributor.authorGe, R
 
dc.contributor.authorRichter, M
 
dc.contributor.authorWoodworth, RC
 
dc.contributor.authorMason, AB
 
dc.contributor.authorHe, QY
 
dc.date.accessioned2008-05-22T04:16:08Z
 
dc.date.available2008-05-22T04:16:08Z
 
dc.date.issued2004
 
dc.description.abstract2D NMR-pH titrations were used to determine pKa values for four conserved tyrosine residues, Tyr45, Tyr85, Tyr96 and Tyr188, in human transferrin. The low pKa of Tyr188 is due to the fact that the iron-binding ligand interacts with Lys206 in open-form and with Lys296 in the closed-form of the protein. Our current results also confirm the anion binding of sulfate and arsenate to transferrin and further suggest that Tyr188 is the actual binding site for the anions in solution. These data indicate that Tyr188 is a critical residue not only for iron binding but also for chelator binding and iron release in transferrin. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
 
dc.description.naturepostprint
 
dc.format.extent381136 bytes
 
dc.format.extent254114 bytes
 
dc.format.mimetypeapplication/pdf
 
dc.format.mimetypeapplication/pdf
 
dc.identifier.citationFebs Letters, 2004, v. 573 n. 1-3, p. 181-185 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.febslet.2004.07.076
 
dc.identifier.citeulike3814034
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.febslet.2004.07.076
 
dc.identifier.epage185
 
dc.identifier.hkuros98457
 
dc.identifier.isiWOS:000223697200031
 
dc.identifier.issn0014-5793
2013 Impact Factor: 3.341
2013 SCImago Journal Rankings: 2.342
 
dc.identifier.issue1-3
 
dc.identifier.openurl
 
dc.identifier.pmid15327995
 
dc.identifier.scopuseid_2-s2.0-4344645436
 
dc.identifier.spage181
 
dc.identifier.urihttp://hdl.handle.net/10722/48523
 
dc.identifier.volume573
 
dc.languageeng
 
dc.languagefre
 
dc.languageger
 
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
 
dc.publisher.placeNetherlands
 
dc.relation.ispartofFEBS Letters
 
dc.relation.referencesReferences in Scopus
 
dc.rightsF E B S Letters. Copyright © Elsevier BV.
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subjectAnion binding
 
dc.subjectBHK, baby-hamster kidney cells
 
dc.subjectHeteronuclear single-quantum coherence nuclear magnetic resonance
 
dc.subjecthTF, human serum transferrin
 
dc.subjecthTF/2N, recombinant N-lobe of human transferrin comprising residues 1-337
 
dc.subjectpK a
 
dc.subjectTransferrin
 
dc.subjectTyrosine
 
dc.titleThe low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. University of Vermont