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 Blackburn, Kenneth D. Karlin

Research output: Contribution to journalArticle

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Abstract

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
Volume129
Issue number17
DOIs
StatePublished - May 2 2007

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histidylhistidine
Absorption spectroscopy
Peptides
Copper
Spectrum Analysis
X-Rays
Carbon Monoxide
X rays
Geometry
X-Ray Absorption Spectroscopy
Ligands
Oxygen
Amyloidogenic Proteins
X ray absorption spectroscopy
Dipeptides
Chelation
Amyloid
Catalytic Domain
Salts
Ions

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Synthesis and x-ray absorption spectroscopy structural studies of Cu(I) complexes of HistidylHistidine peptides : The predominance of linear 2-coordinate geometry. / Himes, Richard A.; Ga, Young Park; Barry, Amanda N.; Blackburn, Ninian; Karlin, Kenneth D.

In: Journal of the American Chemical Society, Vol. 129, No. 17, 02.05.2007, p. 5352-5353.

Research output: Contribution to journalArticle

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