Electrocatalytic CO2 Reduction Catalyzed by Nitrogenase MoFe and FeFe Proteins
Document Type
Article
Journal/Book Title
Bioelectrochemistry
Publication Date
12-5-2017
Publisher
Elsevier BV
Volume
120
First Page
104
Last Page
109
Abstract
Nitrogenases catalyze biological dinitrogen (N2) reduction to ammonia (NH3), and also reduce a number of non-physiological substrates, including carbon dioxide (CO2) to formate (HCOO−) and methane (CH4). Three versions of nitrogenase are known (Mo-, V-, and Fe-nitrogenase), each showing different reactivities towards various substrates. Normally, electrons for substrate reduction are delivered by the Fe protein component of nitrogenase, with energy coming from the hydrolysis of 2 ATP to 2 ADP + 2 Pi for each electron transferred. Recently, it has been demonstrated that energy and electrons can be delivered from an electrode to the catalytic nitrogenase MoFe-protein without the need for Fe protein or ATP hydrolysis. Here, it is demonstrated that both the MoFe- and FeFe-protein can be immobilized as a polymer layer on an electrode and that electron transfer mediated by cobaltocene can drive CO2 reduction to formate in this system. It was also found that the FeFe-protein diverts a greater percentage of electrons to CO2 reduction versus proton reduction compared to the MoFe-protein. Quantification of electron flow to products exhibited Faradaic efficiencies of CO2 conversion to formate of 9% for MoFe protein and 32% for FeFe-protein, with the remaining electrons going to proton reduction to make H2.
Recommended Citation
Hu, B., Harris, D. F., Dean, D. R., Liu, T. L., Yang, Z.-Y., and Seefeldt, L. C. (2018) Electrocatalytic CO2reduction catalyzed by nitrogenase MoFe and FeFe proteins. Bioelectrochemistry120, 104–109.
