Journal
BIOELECTROCHEMISTRY
Volume 120, Issue -, Pages 104-109Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2017.12.002
Keywords
Carbon dioxide; Electrocatalysis; FeFe protein; MoFe protein; Formate
Funding
- Department of Energy, Basic Energy Sciences, Physical Biosciences [DE-SC0010687, DE-SC0010834]
- China Scholarship Council
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Nitrogenases catalyze biological dinitrogen (N-2) 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 H-2. (C) 2017 Elsevier B.V. All rights reserved.
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