期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 58, 期 14, 页码 4601-4605出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201814419
关键词
artificial photosynthesis; carbon dioxide fixation; formate dehydrogenase; interfaces; photocatalysis
资金
- ERC Consolidator Grant MatEnSAP [682833]
- Royal Society [NF160054]
- Christian Doppler Research Association
- OMV Group [SFRH/BD/116515/2016, PTDC/BIA-MIC/2723/2014]
- R&D units - FCT/MCTES [UID/Multi/04551/2013, LISBOA-01-0145-FEDER007660]
- FEDER funds through COMPETE2020/POCI
- European Union's Horizon 2020 research and innovation programme [GA 810856]
- European Research Council (ERC) [682833] Funding Source: European Research Council (ERC)
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据