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Article: Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin
Title | Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin |
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Authors | |
Issue Date | 1996 |
Publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
Citation | Journal Of Biological Chemistry, 1996, v. 271 n. 16, p. 9483-9489 How to Cite? |
Abstract | Large metal ions (>0.9 Å ionic radius) have previously been found to bind only weakly to human serum transferrin (hTF, 80 kDa), presumably because the interdomain cleft cannot close around the metal and synergistic anion. Surprisingly, therefore, we report that Bi3+ (ionic radius 1.03 Å), a metal ion widely used in anti-ulcer drugs, binds strongly to both the N- and C-lobes with log K1* = 19.42 and log K2* = 18.58 (10 mM Hepes, 5 mM bicarbonate, 310 K). The uptake of Bi3+ by apo-hTF from bismuth citrate complexes is very slow (hours), whereas that from bismuth nitrilotriacetate is rapid (minutes). Evidence from absorption and NMR spectroscopy is presented to show that Bi3+ binds to the specific Fe3+ bind-ing sites along with carbonate as the synergistic anion. Under the conditions used, preferential binding of Bi3+to the C-lobe of hTF is observed. Linear free energy relationships show that there is a strong correlation between the strength of binding of Bi3+ and Fe3+ to a wide variety of ligands which include transferrin. Therefore we conclude that the strength of metal ion binding to transferrin is determined more by the ligand donor set than by the size of the ion. |
Persistent Identifier | http://hdl.handle.net/10722/167549 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Li, H | en_US |
dc.contributor.author | Sadler, PJ | en_US |
dc.contributor.author | Sun, H | en_US |
dc.date.accessioned | 2012-10-08T03:08:24Z | - |
dc.date.available | 2012-10-08T03:08:24Z | - |
dc.date.issued | 1996 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 1996, v. 271 n. 16, p. 9483-9489 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167549 | - |
dc.description.abstract | Large metal ions (>0.9 Å ionic radius) have previously been found to bind only weakly to human serum transferrin (hTF, 80 kDa), presumably because the interdomain cleft cannot close around the metal and synergistic anion. Surprisingly, therefore, we report that Bi3+ (ionic radius 1.03 Å), a metal ion widely used in anti-ulcer drugs, binds strongly to both the N- and C-lobes with log K1* = 19.42 and log K2* = 18.58 (10 mM Hepes, 5 mM bicarbonate, 310 K). The uptake of Bi3+ by apo-hTF from bismuth citrate complexes is very slow (hours), whereas that from bismuth nitrilotriacetate is rapid (minutes). Evidence from absorption and NMR spectroscopy is presented to show that Bi3+ binds to the specific Fe3+ bind-ing sites along with carbonate as the synergistic anion. Under the conditions used, preferential binding of Bi3+to the C-lobe of hTF is observed. Linear free energy relationships show that there is a strong correlation between the strength of binding of Bi3+ and Fe3+ to a wide variety of ligands which include transferrin. Therefore we conclude that the strength of metal ion binding to transferrin is determined more by the ligand donor set than by the size of the ion. | en_US |
dc.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.subject.mesh | Bismuth - Chemistry - Metabolism | en_US |
dc.subject.mesh | Cations | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Hydrogen-Ion Concentration | en_US |
dc.subject.mesh | Iron - Metabolism | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Magnetic Resonance Spectroscopy | en_US |
dc.subject.mesh | Metals - Metabolism | en_US |
dc.subject.mesh | Models, Chemical | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Spectrophotometry, Ultraviolet | en_US |
dc.subject.mesh | Thermodynamics | en_US |
dc.subject.mesh | Transferrin - Chemistry - Metabolism | en_US |
dc.title | Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sun, H:hsun@hkucc.hku.hk | en_US |
dc.identifier.authority | Sun, H=rp00777 | en_US |
dc.description.nature | published_or_final_version | en_US |
dc.identifier.doi | 10.1074/jbc.271.16.9483 | - |
dc.identifier.pmid | 8621619 | - |
dc.identifier.scopus | eid_2-s2.0-0029924479 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0029924479&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 271 | en_US |
dc.identifier.issue | 16 | en_US |
dc.identifier.spage | 9483 | en_US |
dc.identifier.epage | 9489 | en_US |
dc.identifier.isi | WOS:A1996UG04400050 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Li, H=14023043100 | en_US |
dc.identifier.scopusauthorid | Sadler, PJ=7103024488 | en_US |
dc.identifier.scopusauthorid | Sun, H=7404827446 | en_US |
dc.identifier.issnl | 0021-9258 | - |