Synthesis and x-ray absorption spectroscopy structural studies of Cu(I) complexes of HistidylHistidine peptides: The predominance of linear 2-coordinate geometry

Richard A. Himes, Young Park Ga, Amanda N. Barry, Ninian J. Blackburn, Kenneth D. Karlin

Research output: Contribution to journalArticle

77 Scopus citations


Modified His-His dipeptides have been reacted with copper(I) salts to model active-site Cu ions bound by contiguous His residues in certain oxygen-activating copper proteins, as well as amyloid β-peptide. Chelation of copper(I) by these ligands affords linear, two-coordinate complexes as studied structurally by X-ray absorption spectroscopy. The complexes are robust toward oxidation, showing limited to no reactivity with O2, and they bind CO weakly. Reaction with a third ligand (N-methylimidazole) affords complexes with a markedly different structure (distorted T-shaped) and reactivity, binding CO and oxidizing rapidly upon exposure to dioxygen.

Original languageEnglish (US)
Pages (from-to)5352-5353
Number of pages2
JournalJournal of the American Chemical Society
Issue number17
StatePublished - May 2 2007


ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this