Integration of Enzymes and Photosensitizers in a Hierarchical Mesoporous Metal–Organic Framework for Light-Driven CO2 Reduction
[1];
[2];
[2];
[2];
[2];
[3];
[4];
[2];
[2];
[2]
- Northwestern Univ., Evanston, IL (United States); CBES
- Northwestern Univ., Evanston, IL (United States)
- Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208-3113, United States
- Northwestern Univ., Evanston, IL (United States); Tianjin Univ. (China). Institute for Molecular Design and Synthesis; Univ. of New South Wales, Sydney, NSW (Australia)
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 photo-induced 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.
- Research Organization:
- Energy Frontier Research Centers (EFRC) (United States). Center for Light Energy Activated Redox Processes (LEAP)
- Sponsoring Organization:
- National Science Foundation (NSF); USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- SC0000989; SC0001059
- OSTI ID:
- 1865071
- Journal Information:
- Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 4 Vol. 142; ISSN 0002-7863
- Publisher:
- American Chemical Society (ACS)Copyright Statement
- Country of Publication:
- United States
- Language:
- English
Similar Records
Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2
Hierarchically Engineered Mesoporous Metal-Organic Frameworks toward Cell-free Immobilized Enzyme Systems