Abstract
We have focused on the catalytic properties of tungsten-containing formate dehydrogenase (FoDH1) from Methylobacterium extorquens AM1 to construct a bioelectrochemical interconversion system between formate (HCOO−) and hydrogen carbonate (HCO3−). FoDH1 catalyzes both of the HCOO oxidation and the HCO3− reduction with several artificial dyes. The bi-molecular reaction rate constants between FoDH1 and the artificial electron acceptors and NAD+ (as the natural electron acceptor) show the property called a linear free energy relationship (LFER), indicating that FoDH1 would have no specificity to NAD+. Similar LFER is also observed for the catalytic reduction of HCO3−. The reversible reaction between HCOO− and HCO3− through FoDH1 has been realized on cyclic voltammetry by using methyl viologen (MV) as a mediator and by adjusting pH from the thermodynamic viewpoint. Potentiometric measurements have revealed that the three redox couples, MV2+/MV·+, HCOO−/HCO3−, FoDH1 (ox/red), reach an equilibrium in the bulk solution when the two-way bioelectrocatalysis proceeds in the presence of FoDH1 and MV. The steady-state voltammograms with two-way bioelectrocatalytic properties are interpreted on a simple model by considering the solution equilibrium.
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