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Formation constants of copper(i) complexes with cysteine, penicillamine and glutathione: implications for copper speciation in the human eye

Königsberger, L.C., Königsberger, E., Hefter, G. and May, P.M. (2015) Formation constants of copper(i) complexes with cysteine, penicillamine and glutathione: implications for copper speciation in the human eye. Dalton Transactions, 44 (47). pp. 20413-20425.

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Link to Published Version: http://dx.doi.org/10.1039/c5dt02129d
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Abstract

Protonation constants for the biologically-important thioamino acids cysteine (CSH), penicillamine (PSH) and glutathione (GSH), and the formation constants of their complexes with Cu(i), have been measured at 25 °C and an ionic strength of 1.00 mol dm-3 (Na)Cl using glass electrode potentiometry. The first successful characterisation of binary Cu(i)-CSH and Cu(i)-GSH species over the whole pH range was achieved in this study by the addition of a second thioamino acid, which prevented the precipitation that normally occurs. Appropriate combinations of binary and ternary (mixed ligand) titration data were used to optimise the speciation models and formation constants for the binary species. The results obtained differ significantly from literature data with respect to the detection and quantification of protonated and polynuclear complexes. The present results are thought to be more reliable because of the exceptionally wide pH and concentration ranges employed, the excellent reproducibility of the data, the close agreement between the calculated and observed formation functions, and the low standard deviations and absence of numerical correlation in the constants. The present formation constants were incorporated into a large Cu speciation model which was used to predict, for the first time, metal-ligand equilibria in the biofluids of the human eye. This simulation provided an explanation for the precipitation of metallic copper in lens and cornea, which is known to occur as a consequence of Wilson's disease.

Publication Type: Journal Article
Murdoch Affiliation: School of Engineering and Information Technology
Publisher: Royal Society of Chemistry
Copyright: © The Royal Society of Chemistry 2015.
URI: http://researchrepository.murdoch.edu.au/id/eprint/29227
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