Rationalization of the strength of metal binding to human serum transferrin

European Journal of Biochemistry

Volumn 242, Issue 2, 1996, Pages 387-393

  Li, Hongyan ^a   Sadler, Peter J ^a,b   Sun, Hongzhe ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

Carbonic anhydrase; Carboxypeptidase; Entatic state; Human serum transferrin; Metal binding

Indexed keywords

APOTRANSFERRIN; SCANDIUM; TRANSFERRIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; IN VITRO STUDY; METAL BINDING; NORMAL HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; ULTRAVIOLET SPECTROPHOTOMETRY;

EID: 0029805818     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0387r.x     Document Type: Article

References (41)

1. Sarra, R., Garratt, R., Gorinsky, B., Jhoti, H. & Lindley, P. F. (1990) High-resolution X-ray studies on rabbit serum transferrin - preliminary structure - analysis of the N-terminal half-molecule at 2.3 Å resolution, Acta Crystallogr. Sect. B 46, 763-771.
2. Zuccola, H. A. (1993) The crystal structure of monoferric human serum transferrin, PhD thesis, Georgia Institute of Technology.
3. Baker, E. N. (1994) Structure and reactivity of transferrin, Adv. Inorg. Chem. 41, 389-463.
4. Grossmann, J. G., Neu, M., Evans, R. W., Lindley, P. F., Appel, H. & Hasnain, S. S. (1993) Metal-induced conformational change in transferrins, J. Mol. Biol. 229, 585-590.
5. Castellano, A. C., Barteri, M., Castagnola, M., Bianconi, A., Borghi, E. & Della Longa, S. (1994) Structure-function relationship in the serotransferrin - the role of the pH on the conformational change and the metal-ions release, Biochem. Biophys. Res. Commun. 198, 646-652.
6. Dautry-Varsat, A. (1986) Receptor-mediated endocytosis: the intracellular journey of transferrin and its receptor, Biochimie (Paris) 68, 375-381.
7. Ward, S. G. & Taylor, R. C. (1988) Anti-tumor activity of the main- group metallic elements: aluminium, gallium, indium, thallium, germanium, lead, antimony and bismuth, in Metal-based anti-tumour drugs (Gielen, M. F., ed.) pp. 1-54, Freund Publishing, House Ltd, London.
8. Harris, W. R., Chen, Y. & Wein, K. (1994) Equilibrium constants for the binding of indium(III) to human serum transferrin, Inorg. Chem. 33, 4991-4998.
9. Battistuzzi, G., Calzolai, L., Messori, L. & Sola, M. (1995) Metal- induced conformational heterogeneity of transferrins: a spectroscopic study of indium(III) and other metal(III)-substituted transferrins, Biochem. Biophys. Res. Commun. 206, 161-170
10. Harris, W. R. & Sheldon, J. (1990) Equilibrium constants for the binding of aluminum to human serum transferrin, Inorg. Chem. 29, 119-124.
11. Kratz, F., Hartmann, M., Keppler, B. & Messori, L. (1994) The binding properties of two antitumor ruthenium(III) complexes to apotransferrin, J. Biol. Chem. 269, 2581-2588.
12. 4+, J. Am. Chem. Soc. 116, 7889-7890.
13. Baxter, G. F. (1989) Bismuth: from alchemy to campylobacter, Pharm. J. 243, 805-810.
14. Chasteen, N. D., White, L. K. & Campbell, R. F. (1977) Metal site conformational states of vanadyl(IV) human serotransferrin complexes, Biochemistry 16, 363-368.
15. 3+) to human serum transferrin, J. Biol. Chem. 271, 9483-9489.
16. Raymond, C. (1981) Physical chemistry with application to biological systems, 2nd edn, pp. 247-251, Macmillan Publishing Co., Inc., New York.
17. Ford-Hutchinson, A. & Perkins, D. (1971) The binding of scandium ions to transferrin in vivo and in vitro, Eur. J. Biochem. 21, 55-59.
18. Aramini, J. M. & Vogel, H. J. (1994) A scandium-45 NMR study of ovotransferrin and its half-molecules, J. Am. Chem. Soc. 116, 1988-1993.
19. Pettit, G. & Pettit, L. D. (1993) IUPAC stability constants database, IUPAC and Academic Software, Otley, United Kingdom.
20. 3+ binding, Biochemistry 32, 3387-3395.
21. Harris, D. C. & Aisen, P. (1989) Physical biochemistry of the transterrins, in Iron carriers and iron proteins (Loehr, T. M., ed.) pp. 239-351, VCH Publishers Inc., Weinheim.
22. Harris, W. R. & Pecoraro, V. L. (1983) Thermodynamic binding constants for gallium transferrin, Biochemistry 22, 292-299.
23. Harris, W. R. (1986) Binding constants for neodymium(III) and samarium(III) with human serum transferrin, Inorg. Chem. 25, 2041-2045.
24. Harris, W. R. (1983) Thermodynamic binding constants of the zinc human serum transferrin complex, Biochemistry 22, 3920-3926.
25. Harris, W. R. (1986) Estimation of the ferrous transferrin binding constants based on thermodynamic studies of nickel(II) transferrin, J. Inorg. Biochem. 27, 41-52.
26. 2+ binding to serum transferrin, J. Inorg. Biochem. 54, 1-19.
27. Bertini, I., Messori, L., Pellacani, G. C. & Sola, M. (1988) Evidence of a metal-synergistic anion bond in thallium(III) transferrin, Inorg. Chem. 27, 761-762.
28. 205Tl as an NMR probe for the investigation of transferrin, J. Am. Chem. Soc. 105, 1347-1350.
29. Aramini, J. M., Krygsman, P. H. & Vogel, H. J. (1994) Thallium-205 and carbon-13 NMR studies of human sero- and chicken ovotransferrin, Biochemistry 33, 3304-3311.
30. Hancock, R. D. & Martell, A. E. (1986) Ligand design for selective complexation of metal ions in aqueous solution, Chem. Rev. 89, 1875-1914.
31. Hancock, R. D. & Martell, A. E. (1995) Lewis acid-base behavior in aqueous solution: some implications for metal ions in biology, Adv. Inorg. Chem. 42, 89-146.
32. Smith, C. A., Anderson, B. F., Baker, H. M. & Baker, E. N. (1992) Metal substitution in transferrin - the crystal-structure of human copper-lactoferrin at 2.1 Å resolution. Biochemistry 31, 4527-4533.
33. Evers, A., Hancock, R. D., Martell, A. E. & Motekaitis, R. J. (1989) Metal-ion recognition in ligands with negatively charged oxygen donor groups - complexation of Fe(III), Ga(III), In(III), Al(III), and other highly charged metal-ions, Inorg. Chem. 28, 2189-2195.
34. Lindskog, S. & Nyman, P. O. (1964) Metal-binding properties of human erythrocyte carbonic anhydrases, Biochim. Biophys. Acta 85, 462-474.
35. Coleman, J. E. & Vallee, B. L. (1961) Metallocarboxypeptidase: stability constants and enzymatic characteristics, J. Biol. Chem. 236, 2244-2249.
36. Eriksson, A. E., Jones, T. A. & Liljas, A. (1988) Refined structure of human carbonic anhydrase-II at 2.0 Å resolution, Proteins Struct. Funct. Genet. 4, 274-282.
37. Rees, D. C., Lewis, M. & Lipscomb, W. N. (1983) Refined crystal structure of carboxypeptidase A at 1.54 Å resolution, J. Mol. Biol. 168, 367-387.
38. Håkansson, K., Carsson, M., Svensson, L. A. & Liljas, A. (1992) Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes, J. Mol. Biol. 227, 1192-1204.
39. Vallee, B. L. & Williams, R. J. P. (1968) Metalloenzymes: the entatic nature of their active sites, Proc. Natl Acad. Sci. USA 59, 498-505.
40. Vallee, B. L., Williams, R. J. P. & Coleman, J. E. (1961) Nitrogen and sulphur at the active centre of carboxypeptidase A, Nature 190, 633-634.
41. Gregory, D. S., Martin, A. C. R., Cheetham, J. C. & Rees, A. R. (1993) The prediction and characterization of metal-binding sites in proteins, Protein Eng. 6, 29-35.