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Issue 5, 2001
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Co-ordination ability towards CuII of the 29-amino acid residue trypsin inhibitor of squash and two of its analogues

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Abstract

Successful application of the potentiometric method together with NMR, EPR, CD and absorption spectroscopy yielded accurate data concerning the stabilities of the complexes formed and their binding modes between CuII and squash trypsin inhibitor. The major residue involved in the metal ion co-ordination is the His-25 imidazole side chain, which acts as an anchoring donor and is bound to metal ion over the whole pH range (3–11.5) studied. The 3N complex with {Nimid, NHis25, NGlu24} binding mode dominates at physiological pH. The data obtained indicate that the protein after a particular mutation could be useful to model metal centres of large proteins.

Graphical abstract: Co-ordination ability towards CuII of the 29-amino acid residue trypsin inhibitor of squash and two of its analogues [ ]

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Supplementary files

Article information


Submitted
01 Nov 2000
Accepted
20 Dec 2000
First published
13 Feb 2001

J. Chem. Soc., Dalton Trans., 2001, 645-652
Article type
Paper

Co-ordination ability towards CuII of the 29-amino acid residue trypsin inhibitor of squash and two of its analogues

P. Mlynarz, D. Valensin, H. Kozlowski, T. Kowalik-Jankowska, J. Otlewski, G. Valensin and N. Gaggelli, J. Chem. Soc., Dalton Trans., 2001, 645
DOI: 10.1039/B008790O

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