| Abstract
| - When contained on a ddab-filmed electrode, the single heme protein myoglobin (Mb) catalyzes the electrochemical reduction of N2O and N3-, as characterized by cyclic voltammetry. Bulk reduction of 15N15NO by Mb/ddab yields 15N15N; reduction of N3- results in formation of ammonia. The reactions are rationalized as two-electron reductions, with the catalyst cycling between the Fe(I) and Fe(III) states of Mb. To our knowledge, this is the first characterization of N2O reduction by an Fe porphyrin or heme protein.
- Myoglobin (Mb), in films of dimethyldidodecylammonium bromide (ddab) on graphite electrodes, is used as acatalyst to mediate the electrochemical reduction of nitrous oxide (N2O) as well as the isoelectronic ion azide(N3-) in aqueous solutions. The electrocatalytic reductions are characterized by a rate-dependent irreversibility incyclic voltammograms of Mb/ddab in the presence of the substrates. Bulk electrolysis shows that the reductionof 15N15NO by Mb/ddab yields 15N15N as shown by GC/MS. The catalytic reduction of azide results in almostquantitative formation of ammonia. These electrocatalytic processes are rationalized as two-electron reductions,with the catalyst cycling between the Fe(I) and Fe(III) states of Mb. To our knowledge, this is the firstcharacterization of N2O reduction by an Fe porphyrin or heme protein.
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