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Article: Integration of Enzymes and Photosensitizers in a Hierarchical Mesoporous Metal-Organic Framework for Light-Driven CO2 Reduction

TitleIntegration of Enzymes and Photosensitizers in a Hierarchical Mesoporous Metal-Organic Framework for Light-Driven CO<inf>2</inf> Reduction
Authors
Issue Date2020
Citation
Journal of the American Chemical Society, 2020, v. 142, n. 4, p. 1768-1773 How to Cite?
AbstractProtection 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.
Persistent Identifierhttp://hdl.handle.net/10722/333412
ISSN
2023 Impact Factor: 14.4
2023 SCImago Journal Rankings: 5.489
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChen, Yijing-
dc.contributor.authorLi, Peng-
dc.contributor.authorZhou, Jiawang-
dc.contributor.authorBuru, Cassandra T.-
dc.contributor.authorAorević, Luka-
dc.contributor.authorLi, Penghao-
dc.contributor.authorZhang, Xuan-
dc.contributor.authorCetin, M. Mustafa-
dc.contributor.authorStoddart, J. Fraser-
dc.contributor.authorStupp, Samuel I.-
dc.contributor.authorWasielewski, Michael R.-
dc.contributor.authorFarha, Omar K.-
dc.date.accessioned2023-10-06T05:19:10Z-
dc.date.available2023-10-06T05:19:10Z-
dc.date.issued2020-
dc.identifier.citationJournal of the American Chemical Society, 2020, v. 142, n. 4, p. 1768-1773-
dc.identifier.issn0002-7863-
dc.identifier.urihttp://hdl.handle.net/10722/333412-
dc.description.abstractProtection 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.-
dc.languageeng-
dc.relation.ispartofJournal of the American Chemical Society-
dc.titleIntegration of Enzymes and Photosensitizers in a Hierarchical Mesoporous Metal-Organic Framework for Light-Driven CO<inf>2</inf> Reduction-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jacs.9b12828-
dc.identifier.pmid31927881-
dc.identifier.scopuseid_2-s2.0-85078661965-
dc.identifier.volume142-
dc.identifier.issue4-
dc.identifier.spage1768-
dc.identifier.epage1773-
dc.identifier.eissn1520-5126-
dc.identifier.isiWOS:000510531900021-

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