Electroreduction of oxygen by cytochrome C oxidase immobilized in electrode-supported lipid bilayer membranes

Cytochrome c oxidase is the terminal enzyme in mammalian respiration, and one of its main functions is to catalyze the reduction of oxygen under physiological conditions. Direct reduction of oxygen at electrodes requires application of substantial overpotentials. In this work, bovine cytochrome c oxidase has been immobilized in electrode-supported lipid bilayer membranes to investigate the electroreduction of oxygen under flow conditions. The effect that temperature, solution pH, and solution composition have on the reduction of oxygen by this novel enzyme-modified electrode is reported. Results indicate that the electroreduction of oxygen is most pronounced at low pH (6.4) and elevated temperature (38 degrees). At an applied potential of -350 mV vs. Ag/AgCl (1M KCl), a current density of ca. 7 microA/cm2 was obtained. The current responses obtained at these electrodes are stable over a period of ca. 10-14 days (10-15% decrease in response). The cytochrome c oxidase-modified electrodes described here could potentially be used for the direct electroreduction of oxygen to water in a biofuel cell.