Issue 2, 2003

Interaction of [RuIII(edta)(H2O)] with amino acids in aqueous solution. Equilibrium, kinetic and protease inhibition studies

Abstract

The interaction of [RuIII(edta)(H2O)] (edta = ethylenediaminetetraacetate) with amino acids, viz. glycine, L-cysteine and S-methylcysteine, was investigated potentiometrically and kinetically. The concentration distribution of various complex species was evaluated as a function of pH. Kinetic data obtained as a function of [amino acid], temperature (5.0 to 45.0 °C) and pressure at a fixed pH of 6.0, reveal that the formation of [RuIII(edta)(Am)] (Am = amino acid) occurs via a rapid amino acid concentration dependent complex-formation reaction of [RuIII(edta)(H2O)], followed by a slow amino acid concentration independent ring-closure step. The kinetic data and activation parameters are interpreted in terms of an associative interchange mechanism and discussed in reference to data reported for closely related systems in the literature. Enzyme inhibition studies revealed that [RuIII(edta)(H2O)] effectively inhibits the cysteine protease activity in papain and bromalein enzymes.

Graphical abstract: Interaction of [RuIII(edta)(H2O)]− with amino acids in aqueous solution. Equilibrium, kinetic and protease inhibition studies

Supplementary files

Article information

Article type
Paper
Submitted
30 Aug 2002
Accepted
01 Nov 2002
First published
10 Dec 2002

Dalton Trans., 2003, 203-209

Interaction of [RuIII(edta)(H2O)] with amino acids in aqueous solution. Equilibrium, kinetic and protease inhibition studies

D. Chatterjee, M. S. A. Hamza, M. M. Shoukry, A. Mitra, S. Deshmukh and R. van Eldik, Dalton Trans., 2003, 203 DOI: 10.1039/B208495N

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