Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6615350 | Electrochimica Acta | 2013 | 8 Pages |
Abstract
The truncated hemoglobin from Bacillus subtilis (trHb-Bs) possesses a surprisingly high affinity for oxygen and resistance to (auto)oxidation; its physiological role in the bacterium is not understood and may be connected with its very special redox and ligand binding reactions. Electron transfer reactions of trHb-Bs were electrochemically studied in solution and at graphite electrodes. Spectrophotometrical potentiometric titration and direct electrochemical measurements gave a heme iron redox potential of â103 ± 4 mV and â108 ± 2 mV vs. NHE, at pH 7, respectively. The redox potential of the heme in trHb-Bs shifted â59 mV per pH unit at pH higher than 7, consistently with a 1eâ/1 H+ - transfer reaction. The heterogeneous rate constant ks for a quasi-reversible 1eâ - 1H+ - transfer reaction between graphite and trHb-Bs was 10.1 ± 2.3 sâ1. Upon reversible cyanide binding the ks doubled, while the redox potential of heme shifted 21 mV negatively, presumably reflecting changes in redox activity and in vivo signaling functions of trHb-Bs associated with ligand binding. Bioelectrocatalytic reduction of O2 catalyzed by trHb-Bs was one of the most efficient hitherto reported for Hbs, with an apparent catalytic rate constant, kcat, of 56 ± 6 sâ1. The results obtained are of particular interest for applications of trHb in environmental biosensing and toxicity screening.
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Authors
Esther Fernandez, Jonas T. Larsson, Kirsty J. McLean, Andrew W. Munro, Lo Gorton, Claes von Wachenfeldt, Elena E. Ferapontova,