Electroreduction of O2 on Cytochrome c Oxidase Modified Electrode for Biofuel Cell

Abstract

Bovine cytochrome c oxidase is immobilized in a gold substrate- supported lipid bilayer membrane to investigate reduction of oxygen using flow through detection technique. The results shown that system temperature, pH and component of solution affect the electroreductive rate of oxygen. In each case the reduction rate of oxygen is controlled by electron transfer. The oxidase modified electrode can be used for the direct electroreduction of oxygen to water in a biofuel cell.

Second Sphere Effects on Oxygen Reduction and Peroxide Activation by Mononuclear Iron Porphyrins and Related Systems

“…The catalytic ORR rate by G65YCu B Mb exceeded those reported for the best artificial synthetic analogues as well as native CcO itself. Efforts on attaching native CcO on electrode similar to bioelectrodes resulted in very sluggish O 2 reduction due to improper alignment of this membrane-bound protein on the electrode, which prevented efficient electron transfer to the active site. , As a result, a CcO-functionalized SAM-covered Au electrode showed <1 μA electrochemical O 2 reduction current at −300 mV, whereas this bioelectrode produced ∼100 μA current at similar potentials …”

“…238,239 As a result, a CcO-functionalized SAMcovered Au electrode showed <1 μA electrochemical O 2 reduction current at −300 mV, whereas this bioelectrode produced ∼100 μA current at similar potentials. 240 To understand the mechanism of facile and selective O 2 reduction catalyzed by the G65YCu B Mb biochemical model, the SERRS-RDE technique was applied. With the help of this , Fe III −OOH, Fe IV �O, and Fe III −OH for which the rates of formation of these species were greater than their rates of decay (Scheme 9).…”

Growth of Phthalocyanine Doped and Undoped Nanotubes Using Mild Synthesis Conditions for Development of Novel Oxygen Reduction Catalysts

“…In an effort to mimic the highly efficient oxygen reduction in biological systems, some researchers have been exploring porphyrin and phthalocyanine metal chelates which are very commonly observed as oxygen transporters and sites of oxygen reduction within cells − . For example, cytochrome c oxidase, which contains a porphyrin macrocycle ring with an iron atom chelated at its center, is the catalyst for oxygen reduction in the outer membrane of mitochondria.…”

“…For example, cytochrome c oxidase, which contains a porphyrin macrocycle ring with an iron atom chelated at its center, is the catalyst for oxygen reduction in the outer membrane of mitochondria. While cytochrome c oxidase works well for mitochondria, its performance ex vivo immobilized on an electrode cannot compare with the performance of a precious metal catalyst (14). There are many reasons why this biomimic lacks performance, one major reason is that it is no longer in a lipid membrane so the orientation and stability of the enzyme is not as controllable.…”