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Zn(2+)-induced deprotonation of a peptide nitrogen in angiotensin I
A P Arnold1, D M Stanley, J G Collins
1Department of Chemistry, University College, University of New South Wales, Australian Defence Force Academy.
FEBS Letters
|September 2, 1991
Abstract:
The interaction of Zn2+ with angiotensin I, a decapeptide containing two histidyl residues, has been studied by 1H-NMR spectroscopy in both water and dimethylsulfoxide. When Zn2+ is added to the peptide in dimethylsulfoxide, binding occurs by coordination of the imidazole rings of both histidines to the metal-ion, enabling the deprotonation of the Phe peptide nitrogen.