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Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO 2
Author(s) -
Chen Yijing,
Li Peng,
Noh Hyunho,
Kung ChungWei,
Buru Cassandra T.,
Wang Xingjie,
Zhang Xuan,
Farha Omar K.
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201901981
Subject(s) - formate , formic acid , formate dehydrogenase , chemistry , cofactor , inorganic chemistry , catalysis , electrochemistry , nuclear chemistry , electrode , organic chemistry , enzyme
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.