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Copper-glutathione Complexes Under Physiological Conditions: Structures in Solution Different from the Solid State Coordination by Jens Z. Pedersen; Christian Steinkühler; Ulrich Weser; Giuseppe Rotilio is a Environmental Science article available to read on EtoBox.

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The physiologically important copper complexes of oxidized glutathione have been examined by electron spin resonance (ESR) spectroscopy in aqueous solution at neutral pH. Low temperature measurements show that the Cu(ll) binding site in oxidized glutathione has the same ligand arrangement as in the copper complexes of S-methylglutathione, glutamine, glutamate and glycine. The site is composed of the amino nitrogens and the carboxyl oxygens of two ?-glutamyl residues; there is no interaction with amide nitrogens, the sulphur bond or the glycyl carboxyl groups. At high metal to ligand ratios a binuclear species exists, in which each Cu(II) binds only to one 7-glutamyl residue. The previously reported forbidden transition detected at g = 4 is due to non-specific aggregation and not to spin coupling of intramolecular sites. Liquid solution ESR spectra show the Cu(II)-glutathione complex has a lower mobility than the corresponding Cu(II)-S-methylglutathione species. From the degree of spectral anisotropy the complex with glutathione is calculated to exist as a dimer. These results demonstrate that the physiologically relevant complex between copper and oxidized glutathione in solution i

Who reads Copper-glutathione Complexes Under Physiological Conditions: Structures in Solution Different from the Solid State Coordination?

Author

Jens Z. Pedersen; Christian Steinkühler; Ulrich Weser; Giuseppe Rotilio

Publisher

Springer Netherlands; Springer-Verlag; Springer Verlag; Kluwer Academic Publishers; Springer Science and Business Media LLC (ISSN 1572-8773)

Published

1996

Language

EN

Field

Environmental Science (Health Sciences)