Document Type
Article
Journal/Book Title
Energy and Environmental Science
Publication Date
6-2016
Volume
9
First Page
2550
Abstract
notrogenase is the only enzyme known to catalyze the reduction of N2 to 2NH3. In vivo, the MoFe protein component of nitrogenase is exclusively reduced by the ATP-hydrolyzing Fe protein in a series of transient association/dissociation steps that are linked to the hyderolysis of two ATP for each electron transeferred. We report MoFe protein immobilized at an electrode surface, where cobaltocene (as an electron mediator that can be observed in real time at a carbon electrode) is used to reduce the MoFe protein (independent of the Fe protein and of ATP hydrolysis) and support the bioelectrocatalytic reduction of protons to dihydrogen, azide to ammonia, and nitrit to ammonia. Bulk bioelectrosynthetic N3 or NO2 reduction (50 mM) for 30 minutes yielded 70 +- 9 nmol NH3 and 234 +- 62 nmol NH3, with NO2 reduction operating at high faradaic efficiency.
Recommended Citation
Milton, Ross D.; Abdellaoui, Sofiene; Khadka, Nimesh; Dean, Dennis R.; Leech, Donal; Seefeldt, Lance C.; and Minteer, Shelley D., "Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein" (2016). Chemistry and Biochemistry Faculty Publications. Paper 683.
https://digitalcommons.usu.edu/chem_facpub/683
