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Natural and Engineered Electron Transfer of Nitrogenase

by Wenyu Gu 1 and Ross D. Milton 2,*
1
Department of Civil and Environmental Engineering, Stanford University, E250 James H. Clark Center, 318 Campus Drive, Stanford, CA 94305, USA
2
Department of Inorganic and Analytical Chemistry, University of Geneva, Sciences II, Quai Ernest-Ansermet 30, 1211 Geneva 4, Switzerland
*
Author to whom correspondence should be addressed.
Chemistry 2020, 2(2), 322-346; https://doi.org/10.3390/chemistry2020021
Received: 8 April 2020 / Revised: 22 April 2020 / Accepted: 23 April 2020 / Published: 27 April 2020
As the only enzyme currently known to reduce dinitrogen (N2) to ammonia (NH3), nitrogenase is of significant interest for bio-inspired catalyst design and for new biotechnologies aiming to produce NH3 from N2. In order to reduce N2, nitrogenase must also hydrolyze at least 16 equivalents of adenosine triphosphate (MgATP), representing the consumption of a significant quantity of energy available to biological systems. Here, we review natural and engineered electron transfer pathways to nitrogenase, including strategies to redirect or redistribute electron flow in vivo towards NH3 production. Further, we also review strategies to artificially reduce nitrogenase in vitro, where MgATP hydrolysis is necessary for turnover, in addition to strategies that are capable of bypassing the requirement of MgATP hydrolysis to achieve MgATP-independent N2 reduction. View Full-Text
Keywords: nitrogenase; ammonia; metalloenzyme; electron transfer; ferredoxin; flavodoxin; Fe protein; MoFe protein nitrogenase; ammonia; metalloenzyme; electron transfer; ferredoxin; flavodoxin; Fe protein; MoFe protein
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Gu, W.; Milton, R.D. Natural and Engineered Electron Transfer of Nitrogenase. Chemistry 2020, 2, 322-346.

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