The monoheme cytochrome c subunit of Alternative Complex III is a direct electron donor to caa3 oxygen reductase in Rhodothermus marinus
Autor: | Filipa Calisto, Manuela M. Pereira, Patrícia N. Refojo, Miguel A. Ribeiro, Miguel Teixeira |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Models Molecular Protein Conformation Protein subunit Clinical Biochemistry Respiratory chain Rhodothermus Electron donor Cytochrome c Group Reductase Biochemistry Electron Transport 03 medical and health sciences chemistry.chemical_compound Electron Transport Complex III Oxidoreductase Cytochromes a3 Cytochrome c oxidase Molecular Biology chemistry.chemical_classification 030102 biochemistry & molecular biology biology Chemistry Cytochrome c Cytochromes a Lipid Metabolism Protein Subunits 030104 developmental biology Coenzyme Q – cytochrome c reductase biology.protein Oxidoreductases |
Zdroj: | Biological chemistry. 398(9) |
ISSN: | 1437-4315 |
Popis: | Alternative Complex III (ACIII) is an example of the robustness and flexibility of prokaryotic respiratory chains. It performs quinol:cytochrome c oxidoreductase activity, being functionally equivalent to the bc1 complex but structurally unrelated. In this work we further explored ACIII investigating the role of its monoheme cytochrome c subunit (ActE). We expressed and characterized the individually isolated ActE, which allowed us to suggest that ActE is a lipoprotein and to show its function as a direct electron donor to the caa3 oxygen reductase. |
Databáze: | OpenAIRE |
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