Aerobic nitrogen-fixing bacteria for hydrogen and ammonium production: current state and perspectives

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17 Scopus citations


Biological nitrogen fixation (BNF) is accomplished through the action of the oxygen-sensitive enzyme nitrogenase. One unique caveat of this reaction is the inclusion of hydrogen gas (H2) evolution as a requirement of the reaction mechanism. In the absence of nitrogen gas as a substrate, nitrogenase will reduce available protons to become a directional ATP-dependent hydrogenase. Aerobic nitrogen-fixing microbes are of particular interest, because these organisms have evolved to perform these reactions with oxygen-sensitive enzymes in an environment surrounded by oxygen. The ability to maintain a functioning nitrogenase in aerobic conditions facilitates the application of these organisms under conditions where most anaerobic nitrogen fixers are excluded. In recent years, questions related to the potential yields of the nitrogenase-derived products ammonium and H2 have grown more approachable to experimentation based on efforts to construct increasingly more complicated strains of aerobic nitrogen fixers such as the obligate aerobe Azotobacter vinelandii. This mini-review provides perspectives of recent and historical efforts to understand and quantify the yields of ammonium and H2 that can be obtained through the model aerobe A. vinelandii, and outstanding questions that remain to be answered to fully realize the potential of nitrogenase in these applications with model aerobic bacteria.

Original languageEnglish (US)
Pages (from-to)1383-1399
Number of pages17
JournalApplied Microbiology and Biotechnology
Issue number4
StatePublished - Feb 1 2020

Bibliographical note

Funding Information:
This work was supported by grants from the MnDRIVE transdisciplinary research initiative through the University of Minnesota based on funding from the state of Minnesota, the National Institute of Food and Agriculture (Project Numbers MIN-12-070 and MIN-12-081), and from the National Science Foundation (CBET-1437758).

Publisher Copyright:
© 2019, Springer-Verlag GmbH Germany, part of Springer Nature.


  • Ammonium
  • Hydrogen
  • Hydrogenase
  • Nitrogenase
  • fixABCX
  • nifL
  • rnf

PubMed: MeSH publication types

  • Journal Article
  • Review


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