Alissandratos, LeeKim, Hye-KyungMatthews, HaydenHennessy, James EPhilbrook, AmyEaston, Christopher2015-12-100099-2240http://hdl.handle.net/1885/69917Recombinant formate dehydrogenase from the acetogen Clostridium carboxidivorans strain P7T, expressed in Escherichia coli, shows particular activity towards NADH-dependent carbon dioxide reduction to formate due to the relative binding affinities of the substrates and products. The enzyme retains activity over 2 days at 4°C under oxic conditions.Author/s retain copyrightKeywords: Carbon dioxide reduction; Formate dehydrogenase; Oxic conditions; Relative binding affinity; Binding energy; Clostridium; Enzyme activity; Escherichia coli; Pollution control; Carbon dioxide; carbon dioxide; formate dehydrogenase; formic acid; formic acid201310.1128/AEM.02886-122016-02-24