Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria
The existence of a complete oxidative phosphorylation system (OXPHOS) supercomplex including both electron transport system and ATP synthases has long been assumed based on functional evidence. However, no structural confirmation of the docking between ATP synthase and proton pumps has been obtained...
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MDPI AG
2021-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/3/1462 |
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| author | Semen Nesterov Yury Chesnokov Roman Kamyshinsky Alisa Panteleeva Konstantin Lyamzaev Raif Vasilov Lev Yaguzhinsky |
| author_facet | Semen Nesterov Yury Chesnokov Roman Kamyshinsky Alisa Panteleeva Konstantin Lyamzaev Raif Vasilov Lev Yaguzhinsky |
| author_sort | Semen Nesterov |
| collection | DOAJ |
| description | The existence of a complete oxidative phosphorylation system (OXPHOS) supercomplex including both electron transport system and ATP synthases has long been assumed based on functional evidence. However, no structural confirmation of the docking between ATP synthase and proton pumps has been obtained. In this study, cryo-electron tomography was used to reveal the supramolecular architecture of the rat heart mitochondria cristae during ATP synthesis. Respirasome and ATP synthase structure in situ were determined using subtomogram averaging. The obtained reconstructions of the inner mitochondrial membrane demonstrated that rows of respiratory chain supercomplexes can dock with rows of ATP synthases forming oligomeric ordered clusters. These ordered clusters indicate a new type of OXPHOS structural organization. It should ensure the quickness, efficiency, and damage resistance of OXPHOS, providing a direct proton transfer from pumps to ATP synthase along the lateral pH gradient without energy dissipation. |
| first_indexed | 2024-03-09T06:07:14Z |
| format | Article |
| id | doaj.art-609f0c0d798e4fef9a7f115fdaa995aa |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T06:07:14Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-609f0c0d798e4fef9a7f115fdaa995aa2023-12-03T12:02:04ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-02-01223146210.3390/ijms22031462Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac MitochondriaSemen Nesterov0Yury Chesnokov1Roman Kamyshinsky2Alisa Panteleeva3Konstantin Lyamzaev4Raif Vasilov5Lev Yaguzhinsky6Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, 123182 Moscow, RussiaKurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, 123182 Moscow, RussiaKurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, 123182 Moscow, RussiaBelozersky Research Institute for Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, RussiaBelozersky Research Institute for Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, RussiaKurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, 123182 Moscow, RussiaMoscow Institute of Physics and Technology, 141701 Dolgoprudny, RussiaThe existence of a complete oxidative phosphorylation system (OXPHOS) supercomplex including both electron transport system and ATP synthases has long been assumed based on functional evidence. However, no structural confirmation of the docking between ATP synthase and proton pumps has been obtained. In this study, cryo-electron tomography was used to reveal the supramolecular architecture of the rat heart mitochondria cristae during ATP synthesis. Respirasome and ATP synthase structure in situ were determined using subtomogram averaging. The obtained reconstructions of the inner mitochondrial membrane demonstrated that rows of respiratory chain supercomplexes can dock with rows of ATP synthases forming oligomeric ordered clusters. These ordered clusters indicate a new type of OXPHOS structural organization. It should ensure the quickness, efficiency, and damage resistance of OXPHOS, providing a direct proton transfer from pumps to ATP synthase along the lateral pH gradient without energy dissipation.https://www.mdpi.com/1422-0067/22/3/1462mitochondriasupercomplexrespirasomeATP synthaseoxidative phosphorylationcryo-electron microscopy |
| spellingShingle | Semen Nesterov Yury Chesnokov Roman Kamyshinsky Alisa Panteleeva Konstantin Lyamzaev Raif Vasilov Lev Yaguzhinsky Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria International Journal of Molecular Sciences mitochondria supercomplex respirasome ATP synthase oxidative phosphorylation cryo-electron microscopy |
| title | Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria |
| title_full | Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria |
| title_fullStr | Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria |
| title_full_unstemmed | Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria |
| title_short | Ordered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria |
| title_sort | ordered clusters of the complete oxidative phosphorylation system in cardiac mitochondria |
| topic | mitochondria supercomplex respirasome ATP synthase oxidative phosphorylation cryo-electron microscopy |
| url | https://www.mdpi.com/1422-0067/22/3/1462 |
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