Erv1 and Cytochrome c Mediate Rapid Electron Transfer via A Collision-Type Interaction
| Autor: | Esra Peker, Alexander Volkov, Jan Riemer, Alican J. Erdogan |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Molecular model Mitochondrial intermembrane space Protein Conformation Oxidative phosphorylation Crystallography X-Ray Electron Transport Fungal Proteins 03 medical and health sciences Electron transfer 0302 clinical medicine Structural Biology Yeasts Oxidoreductases Acting on Sulfur Group Donors Molecular Biology Nuclear Magnetic Resonance Biomolecular 030304 developmental biology chemistry.chemical_classification 0303 health sciences Reactive oxygen species biology Cytochrome c Cytochromes c Nuclear magnetic resonance spectroscopy Oxygen chemistry biology.protein Biophysics Protein folding Oxidation-Reduction 030217 neurology & neurosurgery Protein Binding |
| Zdroj: | Journal of molecular biology. 433(15) |
| ISSN: | 1089-8638 |
| Popis: | Being essential for oxidative protein folding in the mitochondrial intermembrane space, the mitochondrial disulfide relay relies on the electron transfer (ET) from the sulfhydryl oxidase Erv1 to cytochrome c (Cc). Using solution NMR spectroscopy, we demonstrate that while the yeast Cc-Erv1 system is functionally active, no observable binding of the protein partners takes place. The transient interaction between Erv1 and Cc can be rationalized by molecular modeling, suggesting that a large surface area of Erv1 can sustain a fast ET to Cc via a collision-type mechanism, without the need for a canonical protein complex formation. We suggest that, by preventing the direct ET to molecular oxygen (O2), the collision-type Cc-Erv1 interaction plays a role in protecting the organism against reactive oxygen species. |
| Databáze: | OpenAIRE |
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