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Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants

Part of the Structure and Bonding book series (4143,volume 88)

Abstract

Serum transferrin is an 80 kDa glycoprotein which transports Fe3+ and a variety of metal ions of diagnostic, therapeutic and toxic importance. Methods for the study of the differences between the two metal binding sites (the N- and C-lobe sites), and mechanisms for the uptake and release of both metal ions and synergistic anions are discussed. The strength of metal binding to transferrin can be rationalised on the basis of metal ion acidity (strength of hydroxide binding). Similarly the strength of metal binding to the enzymes carbonic anhydrase and carboxypeptidase can be correlated with the binding of the same metal ions to imidazole. Such correlations of metal binding to proteins and low molecular mass ligands may provide insight into the preorganisation of metal binding sites in proteins.

Keywords

  • transferrin
  • carbonic anhydrase
  • carboxypeptidase
  • stability constant
  • metal ions

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Correspondence to Hongzhe Sun or Peter J. Sadler .

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Sun, H., Cox, M.C., Li, H., Sadler, P.J. (1997). Rationalisation of metal binding to transferrin: Prediction of metal-protein stability constants. In: Hill, H.A.O., Sadler, P.J., Thomson, A.J. (eds) Metal Sites in Proteins and Models. Structure and Bonding, vol 88. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-62870-3_3

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