Tyrosinate and lysinate as bridging residues in copper(II) dipeptide complexes

Barbara Radomska, Imre Sovago, Tamas Kiss

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

A pH-metric study, together with some supporting spectroscopy (u.v.-visible, c.d., and e.s.r.), was made on copper(II) complexes of L-phenylalanyl-L-tyrosine, L-tyrosyl-L-phenylalanine, L-lysyl-L-tyrosine, and L-tyrosyl-L-lysine at 25°C and l = 0.2 mol dm-3 (KCl). It was established that in dilute aqueous solutions, besides metal-ligand co-ordination characteristic of simple dipeptides, there are interactions between copper(II) and the side-chain phenolate group of the tyrosine residue and/or the ε-amino group of the lysine residue. In these dimeric species, both the lysine and the tyrosine moieties can behave as bridges between monomeric complexes.

Original languageEnglish
Pages (from-to)289-292
Number of pages4
JournalJournal of the Chemical Society, Dalton Transactions
Issue number1
DOIs
Publication statusPublished - Dec 1 1990

ASJC Scopus subject areas

  • Chemistry(all)

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