Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO2

• DOI: 10.1002/anie.201901981
• Publication Date: 2019-03-26T23:13:32Z
• Authors: Yijing Chen; Peng Li; Hyunho Noh; Chung‐Wei Kung; Cassandra T. Buru; Xingjie Wang; Xuan Zhang; Omar K. Farha
• Keywords: Formate dehydrogenase

The efficient fixation of excess CO2 from the atmosphere to yield value-added chemicals remains crucial in response increasing levels carbon emission. Coupling enzymatic reactions with electrochemical regeneration cofactors is a promising technique for fixing CO2, while producing biomass which can be further transformed into biofuels. Herein, bioelectrocatalytic system was established by depositing crystallites mesoporous metal–organic framework (MOF), termed NU-1006, containing formate dehydrogenase, on fluorine-doped tin oxide glass electrode modified Cp*Rh(2,2′-bipyridyl-5,5′-dicarboxylic acid)Cl2 complex. This converts formic acid at rate 79±3.4 mm h−1 nicotinamide adenine dinucleotide cofactor. MOF–enzyme composite exhibited significantly higher catalyst stability when subjected non-native conditions compared free enzyme, doubling yield.