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Article: N-lobe versus C-lobe complexation of bismuth by human transferrin
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TitleN-lobe versus C-lobe complexation of bismuth by human transferrin
 
AuthorsSun, H1
Li, H1
Mason, AB2
Woodworth, RC2
Sadler, PJ1
 
KeywordsMetal binding
NMR spectroscopy
Protein conformation
Serum protein
Stability constant
 
Issue Date1999
 
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
 
CitationBiochemical Journal, 1999, v. 337 n. 1, p. 105-111 [How to Cite?]
DOI: http://dx.doi.org/10.1042/0264-6021:3370105
 
AbstractInteractions of recombinant N-lobe of human serum transferrin (hTF/2N) with Bi3+, a metal ion widely used in medicine, have been investigated by both UV and NMR spectroscopy. The bicarbonate-independent stability constant for Bi3+ binding (K*) to hTF/2N was determined to be log K* 18.9 ± 0.2 in 5 mM bicarbonate/10 mM Hepes buffer at 310 K, pH 7.4. The presence of Fe3+ in the C-lobe of intact hTF perturbed Bi3+ binding to the N-lobe, whereas binding of Bi3+ to the C-lobe was unaffected by the presence of Fe3+ in the N-lobe. Reactions of Bi3+ (as bismuth nitrilotriacetate or ranitidine bismuth citrate) with hTF/2N in solutions containing 10 mM bicarbonate induced specific changes to high-held 1H-NMR peaks. The 1H co-ordination shifts induced by Bi3+ were similar to those induced by Fe3+ and Ga3+, suggesting that Bi3+ binding causes similar structural changes to those induced by hTF/2N. 13C-NMR data showed that carbonate binds to hTF/2N concomitantly with Bi3+.
 
ISSN0264-6021
2013 Impact Factor: 4.779
 
DOIhttp://dx.doi.org/10.1042/0264-6021:3370105
 
PubMed Central IDPMC1219942
 
ISI Accession Number IDWOS:000078370600015
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSun, H
 
dc.contributor.authorLi, H
 
dc.contributor.authorMason, AB
 
dc.contributor.authorWoodworth, RC
 
dc.contributor.authorSadler, PJ
 
dc.date.accessioned2010-09-06T06:15:24Z
 
dc.date.available2010-09-06T06:15:24Z
 
dc.date.issued1999
 
dc.description.abstractInteractions of recombinant N-lobe of human serum transferrin (hTF/2N) with Bi3+, a metal ion widely used in medicine, have been investigated by both UV and NMR spectroscopy. The bicarbonate-independent stability constant for Bi3+ binding (K*) to hTF/2N was determined to be log K* 18.9 ± 0.2 in 5 mM bicarbonate/10 mM Hepes buffer at 310 K, pH 7.4. The presence of Fe3+ in the C-lobe of intact hTF perturbed Bi3+ binding to the N-lobe, whereas binding of Bi3+ to the C-lobe was unaffected by the presence of Fe3+ in the N-lobe. Reactions of Bi3+ (as bismuth nitrilotriacetate or ranitidine bismuth citrate) with hTF/2N in solutions containing 10 mM bicarbonate induced specific changes to high-held 1H-NMR peaks. The 1H co-ordination shifts induced by Bi3+ were similar to those induced by Fe3+ and Ga3+, suggesting that Bi3+ binding causes similar structural changes to those induced by hTF/2N. 13C-NMR data showed that carbonate binds to hTF/2N concomitantly with Bi3+.
 
dc.description.naturepublished_or_final_version
 
dc.identifier.citationBiochemical Journal, 1999, v. 337 n. 1, p. 105-111 [How to Cite?]
DOI: http://dx.doi.org/10.1042/0264-6021:3370105
 
dc.identifier.doihttp://dx.doi.org/10.1042/0264-6021:3370105
 
dc.identifier.epage111
 
dc.identifier.hkuros43989
 
dc.identifier.isiWOS:000078370600015
 
dc.identifier.issn0264-6021
2013 Impact Factor: 4.779
 
dc.identifier.issue1
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC1219942
 
dc.identifier.pmid9854031
 
dc.identifier.scopuseid_2-s2.0-0032952724
 
dc.identifier.spage105
 
dc.identifier.urihttp://hdl.handle.net/10722/69628
 
dc.identifier.volume337
 
dc.languageeng
 
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofBiochemical Journal
 
dc.relation.referencesReferences in Scopus
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subjectMetal binding
 
dc.subjectNMR spectroscopy
 
dc.subjectProtein conformation
 
dc.subjectSerum protein
 
dc.subjectStability constant
 
dc.titleN-lobe versus C-lobe complexation of bismuth by human transferrin
 
dc.typeArticle
 
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Author Affiliations
  1. University of Edinburgh
  2. University of Vermont