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

The efficient fixation of excess CO₂ 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.