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

F. Kolbe, S. Safarian, Ż. Piórek, S. Welsch, H. Müller and H. Michel ()
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F. Kolbe: Max Planck Institute of Biophysics
S. Safarian: Max Planck Institute of Biophysics
Ż. Piórek: Max Planck Institute of Biophysics
S. Welsch: Max Planck Institute of Biophysics
H. Müller: Max Planck Institute of Biophysics
H. Michel: Max Planck Institute of Biophysics

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-27174-y

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