Abstract
An investigation of oxygen reduction reaction (ORR) catalyzed by microperoxidase-11 (MP-11) at the polarized water/1,2-dichloroethane (DCE) interface is reported. MP-11 contains a heme group covalently bonded to an undecapeptide chain via two thioether bonds of cysteine residues, as in cytochrome c oxidases (CcOs), and has been widely studied as a biomimetic model of CcOs. Herein we demonstrated that MP-11 can adsorb at the water/DCE interface and catalyze the O2 reduction by lipophilic electron donors, namely tetrathiafulvalene (TTF) and 1,1′-dimethylferrocene (DFc). The overall catalytic ORR corresponds to a proton coupled electron transfer (PCET) reaction and is kinetically controlled by the heterogeneous conversion of MP-11 from ferric (FeIII-MP-11) to ferrous state (FeII-MP-11). Given that a significant amount of H2O2 was produced for both electron donors, it indicates that MP-11 has a remarkable impact on the ORR pathway and that MP-11, similar to other mononuclear macrocyclic compounds, cannot sele...
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