Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein
Abstract
Nitrogenase is the only enzyme known to catalyze the reduction ofN2 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 MoFeprotein immobilized at an electrode surface, where cobaltocene (asan 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 bioelectro synthetic 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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 20, 2016
- Accession Number
- AD1058427
Entities
People
- Dennis R Dean
- Dónal Leech
- Lance C. Seefeldt
- Nimesh Khadka
- Ross D Milton
- Shelley D. Minteer
- Sofiène Abdellaoui
Organizations
- University of Utah