Proton transfer in uncoupled variants of cytochrome c oxidase
| Autor: | Ingrid Albertsson, Jóhanna Vilhjálmsdóttir, Peter Brzezinski, Pia Ädelroth, Margareta R. A. Blomberg |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Proton Stereochemistry Protein Conformation Biophysics Protonation medicine.disease_cause Biochemistry Catalysis Electron Transport Complex IV 03 medical and health sciences Electron transfer Bacterial Proteins Structural Biology Catalytic Domain Genetics medicine Cytochrome c oxidase Molecular Biology 030304 developmental biology 0303 health sciences Mutation biology Bacteria Chemistry 030302 biochemistry & molecular biology Energy landscape Biological Transport Cell Biology biology.protein Cytochrome aa3 Protons |
| Zdroj: | FEBS lettersReferences. 594(5) |
| ISSN: | 1873-3468 |
| Popis: | Cytochrome c oxidase is a membrane-bound redox-driven proton pump that harbors two proton-transfer pathways, D and K, which are used at different stages of the reaction cycle. Here, we address the question if a D pathway with a modified energy landscape for proton transfer could take over the role of the K pathway when the latter is blocked by a mutation. Our data indicate that structural alterations near the entrance of the D pathway modulate energy barriers that influence proton transfer to the proton-loading site. The data also suggest that during reduction of the catalytic site, its protonation has to occur via the K pathway and that this proton transfer to the catalytic site cannot take place through the D pathway. |
| Databáze: | OpenAIRE |
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