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dc.contributor.authorGuo, Maolinen
dc.contributor.authorHarvey, Ianen
dc.contributor.authorYang, Weipingen
dc.contributor.authorCoghill, Lorraineen
dc.contributor.authorCampopiano, Dominic Jen
dc.contributor.authorParkinson, John Aen
dc.contributor.authorMacGillivray, Ross T Aen
dc.contributor.authorHarris, Wesley Ren
dc.contributor.authorSadler, Peter Jen
dc.coverage.spatial13en
dc.date.accessioned2005-01-31T16:56:29Z
dc.date.available2005-01-31T16:56:29Z
dc.date.issued2003-10-07
dc.identifier.citationJournal of Biological Chemistry (2003), 278(4), 2490-2502
dc.identifier.urihttp://www.jbc.org
dc.identifier.uriDOI 10.1074/jbc.M208776200
dc.identifier.urihttp://hdl.handle.net/1842/662
dc.description.abstractThe 34-kDa periplasmic iron-transport protein (FBP) from Neisseria gonorrhoeae (nFBP) contains Fe(III) and (hydrogen)phosphate (synergistic anion). It has a characteristic ligand-to-metal charge-transfer absorption band at 481 nm. Phosphate can be displaced by (bi)carbonate to give Fe.CO3.nFBP (lamda max 459 nm). The local structures of native Fe-PO4-nFBP and Fe.CO3.nFBP were determined by EXAFS at the FeK edge using full multiple scattering analysis. The EXAFS analysis reveals that both phosphate and carbonate ligands bind to FBP in monodentate mode in contrast to transferrins, which bind carbonate in bidentate mode. The EXAFS analysis also suggests an alternative to the crystallographically determined position of the Glu ligand, and this in turn suggests that an H-bonding network may help to stabilize monodentate binding of the synergistic anion. The anions oxalate, pyrophosphate, and nitrilotriacetate also appear to serve as synergistic anions but not sulfate or perchlorate. The oxidation of Fe(II) in the presence of nFBP led to a weak Fe(III).nFBP complex (lamda max 471 nm). Iron and phosphate can be removed from FBP at low pH (pH 4.5) in the presence of a large excess of citrate. Apo-FBP is less soluble and less stable than Fe.nFBP and binds relatively weakly to Ga(III) and Bi(III) but not to Co(III) ions, all of which bind strongly to apo-human serum transferrin.en
dc.format.extent277196 bytesen
dc.format.mimetypeapplication/pdfen
dc.language.isoen
dc.publisher© 2003 The American Society for Biochemistry and Molecular Biology, Inc.en
dc.subjectSynergistic actionen
dc.subjectMetal Bindingen
dc.subjectFerric Ion-Binding Proteinen
dc.subjectNeisseria Gonorrhoeaeen
dc.titleSynergistic Anion and Metal Binding to the Ferric Ion-binding Protein from Neisseria gonorrhoeaeen
dc.typeArticleen


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