Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 142, Issue 4, Pages 1768-1773Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b12828
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Funding
- Center for Light Energy Activated Redox Processes (LEAP), an Energy Frontier Research Center - U.S. Department of Energy, Office of Science, Basic Energy Sciences [DE-SC0001059]
- Center for Bio-Inspired Energy Science, an Energy Frontier Research Center - U.S. Department of Energy, Office of Science, Basic Energy Sciences [DE-SC0000989]
- Soft and Hybrid Nanotechnology Experimental (SHyNE) Resource [NSF NNCI-1542205]
- MRSEC program at the Materials Research Center [NSF DMR-1720139]
- International Institute for Nanotechnology (IIN)
- Keck Foundation
- State of Illinois through the IIN
- NSF [CHE-1048773, DMR0521267]
- SHyNE Resource [NSF NNCI-1542205]
- State of Illinois
- IIN
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Protection of enzymes with synthetic materials is a viable strategy to stabilize, and hence to retain, the reactivity of these highly active biomolecules in non-native environments. Active synthetic supports, coupled to encapsulated enzymes, can enable efficient cascade reactions which are necessary for processes like light-driven CO2 reduction, providing a promising pathway for alternative energy generation. Herein, a semi-artificial system-containing an immobilized enzyme, formate dehydrogenase, in a light harvesting scaffold-is reported for the conversion of CO2 to formic acid using white light. The electron-mediator Cp*Rh(2,2'-bipyridyl-5,5'-dicarboxylic acid)Cl was anchored to the nodes of the metal-organic framework NU-1006 to facilitate ultrafast photoinduced electron transfer when irradiated, leading to the reduction of the coenzyme nicotinamide adenine dinucleotide at a rate of about 28 mM.h(-1). Most importantly, the immobilized enzyme utilizes the reduced coenzyme to generate formic acid selectively from CO2 at a high turnover frequency of about 865 h(-1) in 24 h. The outcome of this research is the demonstration of a feasible pathway for solar-driven carbon fixation.
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