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The inner workings of the hydrazine synthase multiprotein complex

Author

Listed:
  • Andreas Dietl

    (Max Planck Institute for Medical Research)

  • Christina Ferousi

    (Institute for Water and Wetland Research, Radboud University Nijmegen)

  • Wouter J. Maalcke

    (Institute for Water and Wetland Research, Radboud University Nijmegen)

  • Andreas Menzel

    (Swiss Light Source, Paul Scherrer Institute)

  • Simon de Vries

    (Delft University of Technology)

  • Jan T. Keltjens

    (Institute for Water and Wetland Research, Radboud University Nijmegen)

  • Mike S. M. Jetten

    (Institute for Water and Wetland Research, Radboud University Nijmegen
    Delft University of Technology)

  • Boran Kartal

    (Institute for Water and Wetland Research, Radboud University Nijmegen
    Laboratory of Microbiology, Gent University)

  • Thomas R. M. Barends

    (Max Planck Institute for Medical Research)

Abstract

Hydrazine is an intermediate in the process of anaerobic ammonium oxidation which has a major role in the Earth’s nitrogen cycle; the crystal structure of a hydrazine synthase enzyme provides insights into the mechanism of hydrazine synthesis.

Suggested Citation

  • Andreas Dietl & Christina Ferousi & Wouter J. Maalcke & Andreas Menzel & Simon de Vries & Jan T. Keltjens & Mike S. M. Jetten & Boran Kartal & Thomas R. M. Barends, 2015. "The inner workings of the hydrazine synthase multiprotein complex," Nature, Nature, vol. 527(7578), pages 394-397, November.
    • Handle: RePEc:nat:nature:v:527:y:2015:i:7578:d:10.1038_nature15517
    DOI: 10.1038/nature15517
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    Cited by:

    1. Beiying Li & Conghe Liu & Jingjing Bai & Yikun Huang & Run Su & Yan Wei & Bin Ma, 2024. "Strategy to mitigate substrate inhibition in wastewater treatment systems," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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