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Copper ions in the active sites of several proteins/enzymes interact with phenols and quinones, and this interaction is associated to the reactivity of the enzymes. In this study the speciation of the Cu 2+  with iminodiacetic phenolate/hydroquinonate ligands has been examined by pH-potentiometry. The results reveal that the iminodiacetic phenol ligand forms mononuclear complexes with Cu 2+  at acidic and alkaline pHs, and a binuclear O phenolate -bridged complex at pH range from 7 to 8.5. The binucleating hydroquinone ligand forms only 2 : 1 metal to ligand complexes in solution. The pK values of the protonation of the phenolate oxygen of the two ligands are reduced about 2 units after complexation with the metal ion and are close to the pK values for the copper-interacting tyrosine phenol oxygen in copper enzymes.

bioinorganic chemistry and applications/bioinorganic chemistry and applications

pH-Potentiometric Investigation towards Chelating Tendencies of<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>p</mml:mi></mml:math>-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes

pH-Potentiometric Investigation towards Chelating Tendencies ofp-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes