کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
7704720 1496893 2018 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Electrocatalytic CO2 reduction catalyzed by nitrogenase MoFe and FeFe proteins
موضوعات مرتبط
مهندسی و علوم پایه شیمی الکتروشیمی
پیش نمایش صفحه اول مقاله
Electrocatalytic CO2 reduction catalyzed by nitrogenase MoFe and FeFe proteins
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioelectrochemistry - Volume 120, April 2018, Pages 104-109
نویسندگان
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