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Coupling enzymatic reactions with electrochemical regeneration of cofactors is a promising technique for fixing CO<jats:sub>2<\/jats:sub>, while producing biomass which can be further transformed into biofuels. Herein, a bioelectrocatalytic system was established by depositing crystallites of a mesoporous metal\u2013organic framework (MOF), termed NU\u20101006, containing formate dehydrogenase, on a fluorine\u2010doped tin oxide glass electrode modified with Cp*Rh(2,2\u2032\u2010bipyridyl\u20105,5\u2032\u2010dicarboxylic acid)Cl<jats:sub>2<\/jats:sub> complex. This system converts CO<jats:sub>2<\/jats:sub> into formic acid at a rate of 79\u00b13.4\u2005m<jats:sc>m\u2009<\/jats:sc>h<jats:sup>\u22121<\/jats:sup> with electrochemical regeneration of the nicotinamide adenine dinucleotide cofactor. The MOF\u2013enzyme composite exhibited significantly higher catalyst stability when subjected to non\u2010native conditions compared to the free enzyme, doubling the formic acid yield.<\/jats:p>","DOI":"10.1002\/anie.201901981","type":"journal-article","created":{"date-parts":[[2019,3,26]],"date-time":"2019-03-26T23:13:32Z","timestamp":1553642012000},"page":"7682-7686","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":154,"title":["Stabilization of Formate Dehydrogenase in a Metal\u2013Organic Framework for Bioelectrocatalytic Reduction of CO<sub>2<\/sub>"],"prefix":"10.1002","volume":"58","author":[{"given":"Yijing","family":"Chen","sequence":"first","affiliation":[{"name":"Department of Chemistry and International Institute of Nanotechnology Northwestern University  2145 Sheridan Road Evanston IL 60208-3113 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