File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1111/j.1432-1033.1996.0387r.x
- Scopus: eid_2-s2.0-0029805818
- PMID: 8973657
- WOS: WOS:A1996VW48500028
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Rationalization of the strength of metal binding to human serum transferrin
Title | Rationalization of the strength of metal binding to human serum transferrin |
---|---|
Authors | |
Keywords | Carbonic anhydrase Carboxypeptidase Entatic state Human serum transferrin Metal binding |
Issue Date | 1996 |
Publisher | Blackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB |
Citation | European Journal Of Biochemistry, 1996, v. 242 n. 2, p. 387-393 How to Cite? |
Abstract | A wide range of metal ions of natural, therapeutic, diagnostic and toxic interest are transported by serum transferrin (80 kDa). It is therefore important to understand the factors that control the strength of metal binding. We show here that even though Sc3+ has only slightly larger ionic radius than Fe3+ (0.075 nm versus 0.065 nm), it binds to the C-lobe and N-lobe sites much more weakly: logK1(*) (bicarbonate-independent binding constant) 14.6 ± 0.2, logK2(*) 13.3 ± 0.3, respectively (10 mM Hepes, 5 mM bicarbonate, 310 K). Preferential binding to the C-lobe was established by 1H-NMR spectroscopy. We show that the strength of binding of divalent and trivalent metal ions to human serum transferrin correlates with metal ion acidity [and therefore with the strength of binding to hydroxide, K1(OH)]. The correlations are of predictive value for a range of other metal ions. The plot of logK1(*) (human serum transferrin) versus logK1(OH) has a negative intercept consistent with unfavorable entropy effects due to lobe closure of apotransferrin on binding of metal ions. This interpretation was tested by comparison with similar correlations of the strength of metal binding to the enzymes carbonic anhydrase and carboxypeptidase with that for the low-M(r) ligand imidazole. These plots have positive intercepts consistent with the preorganized (entatic) state of these metalloenzymes (favorable entropy effects on metal binding). |
Persistent Identifier | http://hdl.handle.net/10722/167546 |
ISSN | |
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 | 2012-10-08T03:08:20Z | - |
dc.date.available | 2012-10-08T03:08:20Z | - |
dc.date.issued | 1996 | en_US |
dc.identifier.citation | European Journal Of Biochemistry, 1996, v. 242 n. 2, p. 387-393 | en_US |
dc.identifier.issn | 0014-2956 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/167546 | - |
dc.description.abstract | A wide range of metal ions of natural, therapeutic, diagnostic and toxic interest are transported by serum transferrin (80 kDa). It is therefore important to understand the factors that control the strength of metal binding. We show here that even though Sc3+ has only slightly larger ionic radius than Fe3+ (0.075 nm versus 0.065 nm), it binds to the C-lobe and N-lobe sites much more weakly: logK1(*) (bicarbonate-independent binding constant) 14.6 ± 0.2, logK2(*) 13.3 ± 0.3, respectively (10 mM Hepes, 5 mM bicarbonate, 310 K). Preferential binding to the C-lobe was established by 1H-NMR spectroscopy. We show that the strength of binding of divalent and trivalent metal ions to human serum transferrin correlates with metal ion acidity [and therefore with the strength of binding to hydroxide, K1(OH)]. The correlations are of predictive value for a range of other metal ions. The plot of logK1(*) (human serum transferrin) versus logK1(OH) has a negative intercept consistent with unfavorable entropy effects due to lobe closure of apotransferrin on binding of metal ions. This interpretation was tested by comparison with similar correlations of the strength of metal binding to the enzymes carbonic anhydrase and carboxypeptidase with that for the low-M(r) ligand imidazole. These plots have positive intercepts consistent with the preorganized (entatic) state of these metalloenzymes (favorable entropy effects on metal binding). | en_US |
dc.language | eng | en_US |
dc.publisher | Blackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB | en_US |
dc.relation.ispartof | European Journal of Biochemistry | en_US |
dc.subject | Carbonic anhydrase | - |
dc.subject | Carboxypeptidase | - |
dc.subject | Entatic state | - |
dc.subject | Human serum transferrin | - |
dc.subject | Metal binding | - |
dc.subject.mesh | Binding Sites | en_US |
dc.subject.mesh | Carbonic Anhydrases - Chemistry | en_US |
dc.subject.mesh | Carboxypeptidases - Chemistry | en_US |
dc.subject.mesh | Humans | 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 | Protein Conformation | en_US |
dc.subject.mesh | Scandium - Metabolism | en_US |
dc.subject.mesh | Spectrophotometry, Ultraviolet | en_US |
dc.subject.mesh | Transferrin - Chemistry - Metabolism | en_US |
dc.title | Rationalization of the strength of metal binding 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 | link_to_OA_fulltext | en_US |
dc.identifier.doi | 10.1111/j.1432-1033.1996.0387r.x | - |
dc.identifier.pmid | 8973657 | - |
dc.identifier.scopus | eid_2-s2.0-0029805818 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0029805818&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 242 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 387 | en_US |
dc.identifier.epage | 393 | en_US |
dc.identifier.isi | WOS:A1996VW48500028 | - |
dc.publisher.place | United Kingdom | 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 | 0014-2956 | - |