期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 141, 期 44, 页码 17498-17502出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b09575
关键词
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资金
- ERC [682833]
- BBSRC [BB/J000124/1, BB/I026367/1]
- EPSRC [EP/L015978/1, EP/G037221/1]
- Marie Curie IntraEuropean Fellowship [PIEF-GA-2013-625034]
- Fundacao para a Ciencia e Tecnologia (Portugal) fellowship [SFRH/BD/116515/2016, PTDC/BIA-MIC/2723/2014, PTDC/BBB-BEP/2885/2014, UID/Multi/04551/2013, LISBOA-01-0145-FEDER-007660]
- European Union [810856]
- FCT/MCTES
- FEDER funds through COMPETE2020/POCI
- European Research Council (ERC) [682833] Funding Source: European Research Council (ERC)
- BBSRC [BB/J000124/1, BB/I026367/1] Funding Source: UKRI
- MRC [MC_UU_00015/2] Funding Source: UKRI
- Fundação para a Ciência e a Tecnologia [PTDC/BBB-BEP/2885/2014, SFRH/BD/116515/2016] Funding Source: FCT
The biological formate hydrogenlyase (FHL) complex links a formate dehydrogenase (FDH) to a hydrogenase (H(2)ase) and produces H-2 and CO2 from formate via mixed-acid fermentation in Escherichia coli. Here, we describe an electrochemical and a colloidal semiartificial FHL system that consists of an FDH and a H(2)ase immobilized on conductive indium tin oxide (ITO) as an electron relay. These in vitro systems benefit from the efficient wiring of a highly active enzyme pair and allow for the reversible conversion of formate to H-2 and CO2 under ambient temperature and pressure. The hybrid systems provide a template for the design of synthetic catalysts and surpass the FHL complex in vivo by storing and releasing H-2 on demand by interconverting CO2/H-2 and formate with minimal bias in either direction.
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