期刊
ACS CATALYSIS
卷 10, 期 6, 页码 3844-3856出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.0c00086
关键词
formate dehydrogenase; CO2 reduction; X-ray structure; oxygen-tolerance; tungsten; molybdopterin; moco
资金
- Fundacao para a Ciencia e Tecnologia (Portugal) [SFRH/BD/116515/2014, PTDC/BBB-EBB/2723/2014, UID/Multi/04551/2013, LISBOA-01-0145-FEDER-007660, UID/Multi/04378/2019]
- FCT/MCTES
- FEDER funds through COMPETE2020/POCI
- European Union [810856]
- Fundação para a Ciência e a Tecnologia [PTDC/BBB-EBB/2723/2014] Funding Source: FCT
Reducing CO2 is a challenging chemical transformation that biology solves easily, with high efficiency and specificity. In particular, formate dehydrogenases are of great interest since they reduce CO2 to formate, a valuable chemical fuel and hydrogen storage compound. The metal-dependent formate dehydrogenases of prokaryotes can show high activity for CO2 reduction. Here, we report an expression system to produce recombinant W/Sec-FdhAB from Desulfovibrio vulgaris Hilden-borough fully loaded with cofactors, its catalytic characterization and crystal structures in oxidized and reduced states. The enzyme has very high activity for CO2 reduction and displays remarkable oxygen stability. The crystal structure of the formate-reduced enzyme shows Sec still coordinating the tungsten, supporting a mechanism of stable metal coordination during catalysis. Comparison of the oxidized and reduced structures shows significant changes close to the active site. The DvFdhAB is an excellent model for studying catalytic CO2 reduction and probing the mechanism of this conversion.
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