Issue 8, 2016

Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

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

Supplementary files

Article information

Article type
Communication
Submitted
18 May 2016
Accepted
20 Jun 2016
First published
20 Jun 2016
This article is Open Access
Creative Commons BY-NC license

Energy Environ. Sci., 2016,9, 2550-2554

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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