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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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Publication details

The article was received on 01 Nov 2000, accepted on 20 Dec 2000 and first published on 13 Feb 2001


Article type: Paper
DOI: 10.1039/B008790O
Citation: J. Chem. Soc., Dalton Trans., 2001,0, 645-652
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    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, 0, 645
    DOI: 10.1039/B008790O

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