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
2011 Impact Factor: 4.897
2011 SCImago Journal Rankings: 0.704
DOIhttp://dx.doi.org/10.1042/0264-6021:3370105
ReferencesReferences in Scopus
DC Field
Value
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.natureLink_to_subscribed_fulltext
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
2011 Impact Factor: 4.897
2011 SCImago Journal Rankings: 0.704
dc.identifier.issue1
dc.identifier.openurl
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.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
Author Affiliations
  1. University of Edinburgh
  2. University of Vermont