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ENZYME MECHANISMS

Nitrogenase loosens its belt to fix dinitrogen

Nature Catalysis volume 5, pages 361–362 (2022)Cite this article

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Nitrogenase reduces dinitrogen at one of its iron–sulfur cores to produce ammonia by a convoluted mechanism. Now, research highlights the importance of sulfur mobility on one of nitrogenase’s metallocofactors for nitrogen fixation.

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Fig. 1: Role of non-physiological reductant dithionite during in vitro nitrogenase catalysis.

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Authors and Affiliations

  1. Department of Inorganic and Analytical Chemistry, Faculty of Sciences, University of Geneva, Geneva, Switzerland

    Ross D. Milton

  2. National Centre of Competence in Research (NCCR) Catalysis, University of Geneva, Geneva, Switzerland

    Ross D. Milton

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  1. Ross D. Milton
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Correspondence to Ross D. Milton.

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The author declares no competing interests.

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Milton, R.D. Nitrogenase loosens its belt to fix dinitrogen. Nat Catal 5, 361–362 (2022). https://doi.org/10.1038/s41929-022-00795-2

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