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Biocatalysis

Iron–sulfur cluster with double duty

Nature Catalysis volume 8, pages 758–759 (2025)Cite this article

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The radical S-adenosylmethionine (SAM) enzyme, AbmM, catalyses a replacement of the ring oxygen of a sugar with sulfur. However, how this reaction takes place is unknown. Now, an [Fe4S4] cluster is shown to have a dual role in catalysis. It functions in the reductive cleavage of SAM and is the donor of the appended sulfur atom.

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Fig. 1: Role of AbmM in the biosynthesis of albomycin.

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Authors and Affiliations

  1. Department of Chemistry, School of Arts and Sciences, University of Pennsylvania, Philadelphia, PA, USA

    Olga A. Esakova & Squire J. Booker

  2. Department of Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA

    Squire J. Booker

  3. Department of Chemistry, The Pennsylvania State University, University Park, PA, USA

    Squire J. Booker

  4. Department of Biochemistry & Molecular Biology, The Pennsylvania State University, University Park, PA, USA

    Squire J. Booker

  5. Howard Hughes Medical Institute, Chevy Chase, MD, USA

    Squire J. Booker

Authors
  1. Olga A. Esakova
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  2. Squire J. Booker
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Correspondence to Squire J. Booker.

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The authors declare no competing interests.

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Esakova, O.A., Booker, S.J. Iron–sulfur cluster with double duty. Nat Catal 8, 758–759 (2025). https://doi.org/10.1038/s41929-025-01386-7

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