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Title: Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2

Abstract

Abstract The efficient fixation of excess CO 2 from the atmosphere to yield value‐added chemicals remains crucial in response to the increasing levels of carbon emission. Coupling enzymatic reactions with electrochemical regeneration of cofactors is a promising technique for fixing CO 2 , while producing biomass which can be further transformed into biofuels. Herein, a bioelectrocatalytic system was established by depositing crystallites of a mesoporous metal–organic framework (MOF), termed NU‐1006, containing formate dehydrogenase, on a fluorine‐doped tin oxide glass electrode modified with Cp*Rh(2,2′‐bipyridyl‐5,5′‐dicarboxylic acid)Cl 2 complex. This system converts CO 2 into formic acid at a rate of 79±3.4 m m  h −1 with electrochemical regeneration of the nicotinamide adenine dinucleotide cofactor. The MOF–enzyme composite exhibited significantly higher catalyst stability when subjected to non‐native conditions compared to the free enzyme, doubling the formic acid yield.

Authors:
 [1];  [2];  [1];  [3];  [1];  [1];  [1]; ORCiD logo [4]
  1. Department of Chemistry and International Institute of Nanotechnology Northwestern University 2145 Sheridan Road Evanston IL 60208-3113 USA
  2. Department of Chemistry and International Institute of Nanotechnology Northwestern University 2145 Sheridan Road Evanston IL 60208-3113 USA, Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials Department of Chemistry Fudan University 2005 Songhu Road Shanghai 200438 China
  3. Department of Chemistry and International Institute of Nanotechnology Northwestern University 2145 Sheridan Road Evanston IL 60208-3113 USA, Department of Chemical Engineering National Cheng Kung University 1 University Road Tainan City 70101 Taiwan
  4. Department of Chemistry and International Institute of Nanotechnology Northwestern University 2145 Sheridan Road Evanston IL 60208-3113 USA, Department of Chemical and Biological Engineering Northwestern University 2145 Sheridan Road Evanston IL 60208-3113 USA
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1510358
Grant/Contract Number:  
SC0001059
Resource Type:
Publisher's Accepted Manuscript
Journal Name:
Angewandte Chemie (International Edition)
Additional Journal Information:
Journal Name: Angewandte Chemie (International Edition) Journal Volume: 58 Journal Issue: 23; Journal ID: ISSN 1433-7851
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
Germany
Language:
English

Citation Formats

Chen, Yijing, Li, Peng, Noh, Hyunho, Kung, Chung‐Wei, Buru, Cassandra T., Wang, Xingjie, Zhang, Xuan, and Farha, Omar K. Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2. Germany: N. p., 2019. Web. doi:10.1002/anie.201901981.
Chen, Yijing, Li, Peng, Noh, Hyunho, Kung, Chung‐Wei, Buru, Cassandra T., Wang, Xingjie, Zhang, Xuan, & Farha, Omar K. Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2. Germany. https://doi.org/10.1002/anie.201901981
Chen, Yijing, Li, Peng, Noh, Hyunho, Kung, Chung‐Wei, Buru, Cassandra T., Wang, Xingjie, Zhang, Xuan, and Farha, Omar K. Thu . "Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2". Germany. https://doi.org/10.1002/anie.201901981.
@article{osti_1510358,
title = {Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2},
author = {Chen, Yijing and Li, Peng and Noh, Hyunho and Kung, Chung‐Wei and Buru, Cassandra T. and Wang, Xingjie and Zhang, Xuan and Farha, Omar K.},
abstractNote = {Abstract The efficient fixation of excess CO 2 from the atmosphere to yield value‐added chemicals remains crucial in response to the increasing levels of carbon emission. Coupling enzymatic reactions with electrochemical regeneration of cofactors is a promising technique for fixing CO 2 , while producing biomass which can be further transformed into biofuels. Herein, a bioelectrocatalytic system was established by depositing crystallites of a mesoporous metal–organic framework (MOF), termed NU‐1006, containing formate dehydrogenase, on a fluorine‐doped tin oxide glass electrode modified with Cp*Rh(2,2′‐bipyridyl‐5,5′‐dicarboxylic acid)Cl 2 complex. This system converts CO 2 into formic acid at a rate of 79±3.4 m m  h −1 with electrochemical regeneration of the nicotinamide adenine dinucleotide cofactor. The MOF–enzyme composite exhibited significantly higher catalyst stability when subjected to non‐native conditions compared to the free enzyme, doubling the formic acid yield.},
doi = {10.1002/anie.201901981},
journal = {Angewandte Chemie (International Edition)},
number = 23,
volume = 58,
place = {Germany},
year = {Thu May 02 00:00:00 EDT 2019},
month = {Thu May 02 00:00:00 EDT 2019}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1002/anie.201901981

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