ArticleScientific reports2022
A critical role of an oxygen-responsive gene for aerobic nitrogenase activity in Azotobacter vinelandii and its application to Escherichia coli.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 31 citations in OpenAlex.
- Engineered diazotrophs with host-inducible nitrogen supply systems: Transforming rice farming through innovative nitrogen biofertilizers.Journal of integrative plant biology · 2026Review
- Enhancement of Nitrogenase Activity in Recombinant Escherichia coli by Replacing Upstream Region of nif Operon from Paenibacillus Species.Chembiochem : a European journal of chemical biology · 2026Article
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- Choreographing root architecture and rhizosphere interactions through synthetic biology.Nature communications · 2024Review
- Polyextremophile engineering: a review of organisms that push the limits of life.Frontiers in microbiology · 2024Review
- Trends in Biological Ammonia Production.Biotech (Basel (Switzerland)) · 2023Review
- Ammonia Production Using Bacteria and Yeast toward a Sustainable Society.Bioengineering (Basel, Switzerland) · 2023Review
- Engineering Nitrogenases for Synthetic Nitrogen Fixation: From Pathway Engineering to Directed Evolution.Biodesign research · 2023Review
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7 authors at 2 institutions in 1 country.
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Abstract
Since nitrogenase is irreversibly inactivated within a few minutes after exposure to oxygen, current studies on the heterologous expression of nitrogenase are limited to anaerobic conditions. This study comprehensively identified genes showing oxygen-concentration-dependent expression only under nitrogen-fixing conditions in Azotobacter vinelandii, an aerobic diazotroph. Among the identified genes, nafU, with an unknown function, was greatly upregulated under aerobic nitrogen-fixing conditions. Through replacement and overexpressing experiments, we suggested that nafU is involved in the maintenance of nitrogenase activity under aerobic nitrogenase activity. Furthermore, heterologous expression of nafU in nitrogenase-producing Escherichia coli increased nitrogenase activity under aerobic conditions by 9.7 times. Further analysis of NafU protein strongly suggested its localization in the inner membrane and raised the possibility that this protein may lower the oxygen concentration inside the cells. These findings provide new insights into the mechanisms for maintaining stable nitrogenase activity under aerobic conditions in A. vinelandii and provide a platform to advance the use of nitrogenase under aerobic conditions.
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