IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v12y2021i1d10.1038_s41467-021-27174-y.html
   My bibliography  Save this article

Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase

Author

Listed:
  • F. Kolbe

    (Max Planck Institute of Biophysics)

  • S. Safarian

    (Max Planck Institute of Biophysics)

  • Ż. Piórek

    (Max Planck Institute of Biophysics
    Phillips University Marburg)

  • S. Welsch

    (Max Planck Institute of Biophysics)

  • H. Müller

    (Max Planck Institute of Biophysics)

  • H. Michel

    (Max Planck Institute of Biophysics)

Abstract

Cytochrome c oxidases are among the most important and fundamental enzymes of life. Integrated into membranes they use four electrons from cytochrome c molecules to reduce molecular oxygen (dioxygen) to water. Their catalytic cycle has been considered to start with the oxidized form. Subsequent electron transfers lead to the E-state, the R-state (which binds oxygen), the P-state (with an already split dioxygen bond), the F-state and the O-state again. Here, we determined structures of up to 1.9 Å resolution of these intermediates by single particle cryo-EM. Our results suggest that in the O-state the active site contains a peroxide dianion and in the P-state possibly an intact dioxygen molecule, the F-state may contain a superoxide anion. Thus, the enzyme’s catalytic cycle may have to be turned by 180 degrees.

Suggested Citation

  • F. Kolbe & S. Safarian & Ż. Piórek & S. Welsch & H. Müller & H. Michel, 2021. "Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27174-y
    DOI: 10.1038/s41467-021-27174-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-021-27174-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-021-27174-y?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. Izumi Ishigami & Raymond G. Sierra & Zhen Su & Ariana Peck & Cong Wang & Frederic Poitevin & Stella Lisova & Brandon Hayes & Frank R. Moss & Sébastien Boutet & Robert E. Sublett & Chun Hong Yoon & Syu, 2023. "Structural insights into functional properties of the oxidized form of cytochrome c oxidase," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Daniel Riepl & Ana P. Gamiz-Hernandez & Terezia Kovalova & Sylwia M. Król & Sophie L. Mader & Dan Sjöstrand & Martin Högbom & Peter Brzezinski & Ville R. I. Kaila, 2024. "Long-range charge transfer mechanism of the III2IV2 mycobacterial supercomplex," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Alex J. Flynn & Svetlana V. Antonyuk & Robert R. Eady & Stephen P. Muench & S. Samar Hasnain, 2023. "A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases," Nature Communications, Nature, vol. 14(1), pages 1-12, 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:12:y:2021:i:1:d:10.1038_s41467-021-27174-y. 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.