Electrochemcial investigation of a multicopper oxidase CueO from E coli

INOR 764

Tao Ye, Chemistry Department, Boston University, 24 Cummington Street, 712, Boston, MA 02215
Here, we present our studies upon a multicopper oxidase CueO, involved in copper homeostasis in Escherichia coli. by the means of protein film voltammetry. A stable, sigmoid-shaped catalytic signal resulted from CueO molecules non-covalently immobilized on the modified gold surface. The oxidase activity assay has been carried out to estimate the kinetic parameters, e.g., kcat and Km towards oxygen. The pH profile of this turnover signals as well as inhibition by azide has been examined in order to gain insight into the electrochemical mechanism of oxygen reduction. Also, two approaches have been utilized to measure the reduction potential of CueO T1 center, which turned out to be around 350mV vs. standard hydrogen electrode (SHE).