Catalytic reduction of dioxygen with modified Thermus thermophilus cytochrome c552.

Efficient catalysis of the oxygen reduction reaction (ORR) is of central importance to function in fuel cells. Metalloproteins, such as laccase (Cu) or cytochrome c oxidase (Cu/Fe-heme) carry out the 4H(+)/4e(-) reduction quite efficiently, but using large, complex protein frameworks. Smaller heme proteins also can carry out ORR, but less efficiently.

Electrocatalytic Dioxygen Reduction by Carbon Electrodes Noncovalently Modified with Iron Porphyrin Complexes: Enhancements from a Single Proton Relay.

Oxygen reduction in acidic aqueous solution mediated by a series of asymmetric iron (III)-tetra(aryl)porphyrins adsorbed to basal- and edge- plane graphite electrodes is investigated. The asymmetric iron porphyrin systems bear phenyl groups at three meso positions and either a 2-pyridyl, a 2-benzoic acid, or a 2-hydroxyphenyl group at the remaining meso position. The presence of the three unmodified phenyl groups makes the compounds insoluble in water, enabling catalyst retention during electrochemical experiments.