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

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.

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 Creators:
Kolbe, Felix1, Author              
Safarian, Schara1, Author              
Piórek, Żaneta1, Author              
Welsch, Sonja2, Author              
Müller, Hanne1, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society, ou_3249263              

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Free keywords: Cryoelectron microscopy; Enzyme mechanisms; Membrane proteins
 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.

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Language(s): eng - English
 Dates: 2021-07-092021-10-292021-11-25
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-27174-y
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 12 Sequence Number: 6903 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723