Journal
CATALYSTS
Volume 12, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/catal12080844
Keywords
bioelectrocatalysis; nitrogen reduction; green ammonia
Categories
Funding
- CSIRO Hydrogen Energy Systems Future Science Platform
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Ammonia is industrially produced from dinitrogen and dihydrogen using high temperature and pressure, while nitrogenase enzymes in biology can operate at ambient conditions. Recent studies have shown the possibility of ATP-free ammonia production by nitrogenase, but the reaction rates are lower and a better understanding of the role of ATP is needed.
Ammonia (NH3) is produced industrially by the Haber-Bosch process from dinitrogen (N-2) and dihydrogen (H-2) using high temperature and pressure with an iron catalyst. In contrast to the extreme conditions used in the Haber-Bosch process, biology has evolved nitrogenase enzymes, which operate at ambient temperature and pressure. In biological settings, nitrogenase requires large amounts of energy in the form of ATP, using at least 13 GJ ton(-1) of ammonia. In 2016, Brown et al. reported ATP-free ammonia production by nitrogenase. This result led to optimism that the energy demands of nitrogenase could be reduced. More recent reports confirmed the ATP-free production of ammonia; however, the rates of reaction are at least an order of magnitude lower. A more detailed understanding of the role of ATP in nitrogenase catalysis is required to develop ATP-free catalytic systems with higher ammonia production rates. Finally, we calculated the theoretical maximal ammonia production rate by nitrogenase and compared it to currently used Haber-Bosch catalysts. Somewhat surprisingly, nitrogenase has a similar theoretical maximum rate to the Haber-Bosch catalysts; however, strategies need to be developed to allow the enzyme to maintain operation at its optimal rate.
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