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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
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    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. 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.

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