Synthesis and X-ray Absorption Spectroscopy Structural Studies of Cu(I) Complexes of HistidylHistidine Peptides: The Predominance of Linear 2-Coordinate Geometry
Journal of the American Chemical Society2007Vol. 129(17), pp. 5352–5353
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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.
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