Journal
ELECTROCHIMICA ACTA
Volume 110, Issue -, Pages 86-93Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.electacta.2013.03.025
Keywords
Heme proteins; Electron transfer; Bacillus subtilis truncated hemoglobin; Bioelectrocatalysis; Ligand binding
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Funding
- Danish Council for Independent Research, Natural Sciences (FNU) [11-107176]
- Swedish Research Council [2010-5031]
- Crafoord Foundation and the Carl Tryggers foundation
- Royal Society (UK)
- Leverhulme Trust Senior Research Fellowship
- Biotechnology and Biological Sciences Research Council (BBSRC, UK)
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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 -103 +/- 4 mV and -108 +/- 2 mV vs. NHE, at pH 7, respectively. The redox potential of the heme in trHb-Bs shifted -59 mV per pH unit at pH higher than 7, consistently with a 1e(-)/1H(+) - transfer reaction. The heterogeneous rate constant k(s), for a quasi-reversible 1e(-)-1H(+) - transfer reaction between graphite and trHb-Bs was 10.1 +/- 2.3 s(-1). 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 O-2 catalyzed by trHb-Bs was one of the most efficient hitherto reported for Hbs, with an apparent catalytic rate constant, k(cat), of 56 +/- 6s(-1). The results obtained are of particular interest for applications of trHb in environmental biosensing and toxicity screening. (C) 2013 Elsevier Ltd. All rights reserved.
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