title: The binding of copper(II) and zinc(II) to oxidized glutathione.
abstract: 1H and 13C NMR studies of Zn(II) binding to oxidized glutathione (GSSG) in aqueous solution over the pH range 4-11 show that it forms a complex with a 1:1 Zn:GSSG stoichiometry. At pH values between 6 and 11 the metal ligands are the COO- and NH2 groups of the glutamate residues. Below pH 5 the glycine end of the molecule also binds to the metal ions. EPR and visible absorption spectra of Cu(II) GSSG solutions suggest that similar complexes are formed with Cu(II). The solid products obtained from these solutions are shown by analysis and EPR to be primarily binuclear with Cu2GSSG stoichiometry, although the structures depend on the pH and stoichiometry of the solution from which they were obtained.
mesh_terms: D003300:Copper; D004578:Electron Spin Resonance Spectroscopy; D005978:Glutathione / Q000031:analogs & derivatives*; D019803:Glutathione Disulfide; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D015032:Zinc
chemical_list: D003300:Copper; D005978:Glutathione; D015032:Zinc; D019803:Glutathione Disulfide