Zn(2+)-induced deprotonation of a peptide nitrogen in angiotensin I.
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.
Arnold
A P
AP
Department of Chemistry, University College, University of New South Wales, Australian Defence Force Academy.
Stanley
D M
DM
Collins
J G
JG
D000595:Amino Acid Sequence; D000803:Angiotensin I / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011522:Protons; D015032:Zinc / Q000737:chemistry*
D010455:Peptides; D011522:Protons; D000803:Angiotensin I; D015032:Zinc; D009584:Nitrogen