Catalytic protein film electrochemistry provides a direct measure of the tetrathionate/thiosulfate reduction potential

Julia M. Kurth, Christiane Dahl, Julea N. Butt

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Abstract

The tetrathionate/thiosulfate interconversion is a two-electron process: S4O62- + 2 e- ↔ 2 S2O32-. Both transfor¬mations can sup-port bacterial growth since S2O32- provides an energy source while S4O62- serves as respiratory electron acceptor. Interest in the corresponding S2O32- oxidation also arises from its widespread use in volumetric analysis of oxidizing agents and bleach neutralization during water-treatment. Here we report protein film electrochemistry that defines the reduction potential of the S4O62-/S2O32- couple. The relevant interconversion is not reversible at inert electrodes. However, facile reduction of S4O62- to S2O32- and the reverse reaction are catalyzed by enzymes of the thiosulfate dehydro¬genase, TsdA, family adsorbed on graphite electrodes. Zero-current potentials measured with different enzymes, at three pH values, and multiple S4O62- and S2O32- con-centrations together with the relevant Nernst equation resolved the tetrathionate/thiosulfate reduction potential as +198 ± 4 mV versus SHE. This potential lies in the approximately 250 mV window encompassing previously reported values calculated from parameters including the free energy of formation. However, the value is considerably more positive than widely used in discussions of bacterial bioenergetics. As a consequence anaerobic respiration by tetrathionate reduction is likely to be more prevalent than presently thought in tetra¬thionate-containing environments such as marine sediments and the human gut.
Original languageEnglish
Pages (from-to)13232–13235
JournalJournal of the American Chemical Society
Volume137
Issue number4
Early online date5 Oct 2015
DOIs
Publication statusPublished - 21 Oct 2015

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