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
2011 Impact Factor: 3.538
2011 SCImago Journal Rankings: 0.484
DOIhttp://dx.doi.org/10.1016/j.febslet.2004.07.076
ISI Accession Number IDWOS:000223697200031
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 3.538
2011 SCImago Journal Rankings: 0.484
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
Author Affiliations
  1. The University of Hong Kong
  2. University of Vermont