IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms10902.html
   My bibliography  Save this article

Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

Author

Listed:
  • Thomas Spatzal

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
    Howard Hughes Medical Institute, California Institute of Technology)

  • Julia Schlesier

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg)

  • Eva-Maria Burger

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg)

  • Daniel Sippel

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg)

  • Limei Zhang

    (California Institute of Technology)

  • Susana L.A. Andrade

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
    BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-Universität Freiburg)

  • Douglas C. Rees

    (Howard Hughes Medical Institute, California Institute of Technology)

  • Oliver Einsle

    (Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg
    BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-Universität Freiburg)

Abstract

The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while its reactivity and electronic structure remain under debate. Here we show that for its resting S=3/2 state the common iron oxidation state assignments must be reconsidered. By a spatially resolved refinement of the anomalous scattering contributions of the 7 Fe atoms of FeMoco, we conclude that three irons (Fe1/3/7) are more reduced than the other four (Fe2/4/5/6). Our data are in agreement with the recently revised oxidation state assignment for the molybdenum ion, providing the first spatially resolved picture of the resting-state electron distribution within FeMoco. This might provide the long-sought experimental basis for a generally accepted theoretical description of the cluster that is in line with available spectroscopic and functional data.

Suggested Citation

  • Thomas Spatzal & Julia Schlesier & Eva-Maria Burger & Daniel Sippel & Limei Zhang & Susana L.A. Andrade & Douglas C. Rees & Oliver Einsle, 2016. "Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement," Nature Communications, Nature, vol. 7(1), pages 1-7, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10902
    DOI: 10.1038/ncomms10902
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms10902
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms10902?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Lorenz Heidinger & Kathryn Perez & Thomas Spatzal & Oliver Einsle & Stefan Weber & Douglas C. Rees & Erik Schleicher, 2024. "Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10902. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.