Structural insights into the catalytic binuclear center of cytochrome c oxidase from Paracoccus denitrificans
- 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.
Author: | Felix Martin Kolbe |
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URN: | urn:nbn:de:hebis:30:3-669553 |
DOI: | https://doi.org/10.21248/gups.66955 |
Place of publication: | Frankfurt am Main |
Referee: | Clemens Glaubitz, Hartmut Michel |
Advisor: | Hartmut Michel |
Document Type: | Doctoral Thesis |
Language: | English |
Date of Publication (online): | 2022/02/22 |
Year of first Publication: | 2021 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Granting Institution: | Johann Wolfgang Goethe-Universität |
Date of final exam: | 2022/02/21 |
Release Date: | 2022/03/16 |
Page Number: | 109 |
HeBIS-PPN: | 491802234 |
Institutes: | Biochemie, Chemie und Pharmazie |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Sammlungen: | Universitätspublikationen |
Licence (German): | ![]() |