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Nitrogenases

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Metalloproteins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1876))

Abstract

Biological nitrogen fixation, the conversion of dinitrogen (N2) into ammonia (NH3), stands as a particularly challenging chemical process. As the entry point into a bioavailable form of nitrogen, biological nitrogen fixation is a critical step in the global nitrogen cycle. In Nature, only one enzyme, nitrogenase, is competent in performing this reaction. Study of this complex metalloenzyme has revealed a potent substrate reduction system that utilizes some of the most sophisticated metalloclusters known. This chapter discusses the structure and function of nitrogenase, covers methods that have proven useful in the elucidation of enzyme properties, and provides an overview of the three known nitrogenase variants.

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Acknowledgments

The authors are supported by the National Institutes of Health grant GM67626 (to M.W.R. and Y.H.).

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA

    Nathaniel S. Sickerman, Yilin Hu & Markus W. Ribbe

  2. Department of Chemistry, University of California, Irvine, Irvine, CA, USA

    Markus W. Ribbe

Authors
  1. Nathaniel S. Sickerman
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  2. Yilin Hu
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  3. Markus W. Ribbe
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Corresponding authors

Correspondence to Yilin Hu or Markus W. Ribbe .

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Editors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California-Irvine, Irvine, CA, USA

    Yilin Hu

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Sickerman, N.S., Hu, Y., Ribbe, M.W. (2019). Nitrogenases. In: Hu, Y. (eds) Metalloproteins. Methods in Molecular Biology, vol 1876. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8864-8_1

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  • DOI: https://doi.org/10.1007/978-1-4939-8864-8_1

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