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

MPG-Autoren
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Kolbe,  Felix
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Safarian,  Schara       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Piórek,  Żaneta
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Welsch,  Sonja       
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

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Müller,  Hanne
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Kolbe, F., Safarian, S., Piórek, Ż., Welsch, S., Müller, H., & Michel, H. (2021). Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase. Nature Communications, 12: 6903. doi:10.1038/s41467-021-27174-y.


Zitierlink: https://hdl.handle.net/21.11116/0000-0009-8680-E
Zusammenfassung
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.