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Issue 8, 2016
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Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

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Abstract

Nitrogenase 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 hydrolysis of two ATP for each electron transferred. 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 nitrite 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.

Graphical abstract: Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

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Publication details

The article was received on 18 May 2016, accepted on 20 Jun 2016 and first published on 20 Jun 2016


Article type: Communication
DOI: 10.1039/C6EE01432A
Citation: Energy Environ. Sci., 2016,9, 2550-2554
  • Open access: Creative Commons BY-NC license
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    Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

    R. D. Milton, S. Abdellaoui, N. Khadka, D. R. Dean, D. Leech, L. C. Seefeldt and S. D. Minteer, Energy Environ. Sci., 2016, 9, 2550
    DOI: 10.1039/C6EE01432A

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