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Updated: Jan 29, 2026

A Method to Manipulate Surface Tension of a Liquid Metal via Surface Oxidation and Reduction
Published on: January 26, 2016
Interfacing Formate Dehydrogenase with Metal Oxides for the Reversible Electrocatalysis and Solar-Driven Reduction of
Melanie Miller1, William E Robinson1, Ana Rita Oliveira2
1Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Abstract:
The integration of enzymes with synthetic materials allows efficient electrocatalysis and production of solar fuels. Here, we couple formate dehydrogenase (FDH) from Desulfovibrio vulgaris Hildenborough (DvH) to metal oxides for catalytic CO2 reduction and report an in-depth study of the resulting enzyme-material interface. Protein film voltammetry (PFV) demonstrates the stable binding of FDH on metal-oxide electrodes and reveals the reversible and selective reduction of CO2 to formate. Quartz crystal microbalance (QCM) and attenuated total reflection infrared (ATR-IR) spectroscopy confirm a high binding affinity for FDH to the TiO2 surface. Adsorption of FDH on dye-sensitized TiO2 allows for visible-light-driven CO2 reduction to formate in the absence of a soluble redox mediator with a turnover frequency (TOF) of 11±1 s-1 . The strong coupling of the enzyme to the semiconductor gives rise to a new benchmark in the selective photoreduction of aqueous CO2 to formate.
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