Structural changes at the surface of cytochrome c oxidase alter the proton-pumping stoichiometry
| Autor: | Johan Berg, Emelie Svahn, Shelagh Ferguson-Miller, Peter Brzezinski, Jian Liu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Protein subunit Biophysics Respiratory chain Rhodobacter sphaeroides Biochemistry Article Protein Structure Secondary Electron Transport Complex IV 03 medical and health sciences Electron transfer Bacterial Proteins Oxidoreductase Cytochrome c oxidase chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry Cell Biology biology.organism_classification 030104 developmental biology Enzyme biology.protein Stoichiometry |
| Zdroj: | Biochim Biophys Acta Bioenerg |
| Popis: | Data from earlier studies showed that minor structural changes at the surface of cytochrome c oxidase, near one of the proton-input pathways (the D pathway), result in dramatically decreased activity and a lower proton-pumping stoichiometry. To further investigate how changes around the D pathway orifice influence functionality of the enzyme, here we modified the nearby C-terminal loop of subunit I of the Rhodobacter sphaeroides cytochrome c oxidase. Removal of 16 residues form this flexible surface loop resulted in a decrease in the proton-pumping stoichiometry to |
| Databáze: | OpenAIRE |
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