1. Stabilization of Formate Dehydrogenase in a Metal-Organic Framework for Bioelectrocatalytic Reduction of CO 2 .
- Author
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Chen Y, Li P, Noh H, Kung CW, Buru CT, Wang X, Zhang X, and Farha OK
- Subjects
- 2,2'-Dipyridyl chemistry, Carbon Dioxide chemistry, Catalysis, Enzyme Stability, Formates chemistry, Glass chemistry, Metal-Organic Frameworks chemistry, Oxidation-Reduction, Tin Compounds chemistry, Carbon Dioxide metabolism, Electrodes, Formate Dehydrogenases chemistry, Formate Dehydrogenases metabolism, Formates metabolism, Metal-Organic Frameworks metabolism, NAD metabolism
- 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 CO2 , 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)Cl2 complex. This system converts CO2 into formic acid at a rate of 79±3.4 mm 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., (© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)- Published
- 2019
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