Zn(2+)-induced deprotonation of a peptide nitrogen in angiotensin I

FEBS Lett. 1991 Sep 2;289(1):96-8. doi: 10.1016/0014-5793(91)80916-q.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensin I / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Nitrogen / chemistry*
  • Peptides / chemistry
  • Protons
  • Zinc / chemistry*


  • Peptides
  • Protons
  • Angiotensin I
  • Zinc
  • Nitrogen