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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Bibliographic Details
Published in:International journal of molecular sciences 2021-02, Vol.22 (3), p.1462
Main Authors: Nesterov, Semen, Chesnokov, Yury, Kamyshinsky, Roman, Panteleeva, Alisa, Lyamzaev, Konstantin, Vasilov, Raif, Yaguzhinsky, Lev
Format: Article
Language:English
Subjects:
Animals
ATP synthase
Cristae
cryo-electron microscopy
Cryoelectron Microscopy
Electron Transport
Enzymes
Heart
Laboratory animals
Mitochondria
Mitochondria, Heart - metabolism
Mitochondria, Heart - ultrastructure
Mitochondrial Membranes - metabolism
Mitochondrial Membranes - ultrastructure
Mitochondrial Proton-Translocating ATPases - metabolism
Mitochondrial Proton-Translocating ATPases - ultrastructure
Oxidative Phosphorylation
Phosphorylation
Protein Conformation
Proteins
Proton Pumps - metabolism
Proton Pumps - ultrastructure
Pumps
Rats
Rats, Wistar
respirasome
supercomplex
Transportation systems
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms22031462