Journal article

Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli

Simon C Drew, Karrera Y Djoko, Lianyi Zhang, Melissa Koay, John F Boas, John R Pilbrow, Zhiguang Xiao, Kevin J Barnham, Anthony G Wedd

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | SPRINGER | Published : 2008

Abstract

Continuous-wave and pulsed electron paramagnetic resonance have been applied to the study of the Cu(II) site of the copper-resistance protein PcoC from Escherichia coli and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands, His1 and His92, at the Cu(II) site of wild-type PcoC, consistent with the available X-ray crystallographic data for the homolog CopC (67% sequence identity) from Pseudomonas syringae pv. tomato. The variants H1F and H92F each lack one of the histidine residues close to the Cu(II) site. The ESEEM data suggest that the surviving histidine residue remains as a ligand. The nA variant features an ext..

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