Pentaglycine-NiII complex: From kinetics to structure

Zeev Gaisin, Gary Gellerman, Dan Meyerstein

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Binding NiII to the terminal amine of a peptide depresses totally its nucleophilic character as measured by the rate constant of the reaction of the peptide with 4-nitrophenyl acetate. The structure of Ni II(GGGGG) in aqueous solutions was determined by this technique. The results indicate that the ratio of complexes in which the nickel is bound to four deprotonated peptide nitrogen atoms to those in which the nickel is bound to the terminal amine and three deprotonated peptide nitrogen atoms increases as the pH increases. At pH 9.0, this ratio is approximately 1. We measured the nucleophilic properties of the terminal amine of a Ni(peptide) complex as a tool to elucidate the ligation sites of the cation.

Original languageEnglish
Pages (from-to)3191-3194
Number of pages4
JournalEuropean Journal of Inorganic Chemistry
Issue number18
StatePublished - 1 Jan 2013


  • Amines
  • Kinetics
  • Nickel
  • Nucleophiles
  • Peptides

ASJC Scopus subject areas

  • Inorganic Chemistry


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