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
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
الکتروشیمی
پیش نمایش صفحه اول مقاله
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 (HCOOâ) 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 ADPÂ +Â 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
Journal: Bioelectrochemistry - Volume 120, April 2018, Pages 104-109
نویسندگان
Bo Hu, Derek F. Harris, Dennis R. Dean, T. Leo Liu, Zhi-Yong Yang, Lance C. Seefeldt,