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Danyi, Péter and Várnagy, Katalin and Sóvágó, Imre and Schön, István and Sanna, Daniele and Micera, Giovanni (1995) Potentiometric and spectroscopic studies on the copper(II) complexes of peptide hormones containing disulfide bridges. Journal of Inorganic Biochemistry, Vol. 60 (1), p. 69-78. ISSN 0162-0134. Article. Full text not available from this repository. DOI: 10.1016/0162-0134(95)00003-7 AbstractCopper(II) complexes of oxytocin, 4-Glu-oxytocin, 5-Asp-oxytocin, and GlyGlyGly-Lys8-vasopressin were studied by potentiometric, EPR, and UV-visible spectroscopic methods. The formation of 4N-coordinated complexes was characteristic of all ligands. This type of coordination is especially favored for oxytocin due to the specific conformation of the ring coupled by the disulfide bridge. The coordination of the γ-carboxylate group of 4-Glu-oxytocin and a disulfide sulfur atom of GlyGlyGly-Lys8-vasopressin was reported to occur in the 2N-complexes over medium pH range.
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