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pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes
by
Chryssoula Drouza
, Anastasios D. Keramidas
, Marios Stylianou
in
Agricultural production
/ Binding sites
/ Complexation
/ Copper
/ Electrodes
/ Enzymes
/ Hydroquinone
/ Ligands
/ Phenol
/ Quinones
/ Solution chemistry
/ Speciation
/ Spectrum analysis
/ Studies
2010
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pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes
by
Chryssoula Drouza
, Anastasios D. Keramidas
, Marios Stylianou
in
Agricultural production
/ Binding sites
/ Complexation
/ Copper
/ Electrodes
/ Enzymes
/ Hydroquinone
/ Ligands
/ Phenol
/ Quinones
/ Solution chemistry
/ Speciation
/ Spectrum analysis
/ Studies
2010
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pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes
by
Chryssoula Drouza
, Anastasios D. Keramidas
, Marios Stylianou
in
Agricultural production
/ Binding sites
/ Complexation
/ Copper
/ Electrodes
/ Enzymes
/ Hydroquinone
/ Ligands
/ Phenol
/ Quinones
/ Solution chemistry
/ Speciation
/ Spectrum analysis
/ Studies
2010
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pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes
Journal Article
pH-Potentiometric Investigation towards Chelating Tendencies of p-Hydroquinone and Phenol Iminodiacetate Copper(II) Complexes
2010
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Overview
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 Cu2+ with iminodiacetic phenolate/hydroquinonate ligands has been examined by pH-potentiometry. The results reveal that the iminodiacetic phenol ligand forms mononuclear complexes with Cu2+ at acidic and alkaline pHs, and a binuclear Ophenolate-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.
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