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TitleOrdered Clusters of the Complete Oxidative Phosphorylation System in Cardiac Mitochondria.
Journal, issue, pagesInt J Mol Sci, Vol. 22, Issue 3, Year 2021
Publish dateFeb 2, 2021
AuthorsSemen Nesterov / Yury Chesnokov / Roman Kamyshinsky / Alisa Panteleeva / Konstantin Lyamzaev / Raif Vasilov / Lev Yaguzhinsky /
PubMed AbstractThe 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. ...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.
External linksInt J Mol Sci / PubMed:33540542 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution27.7 - 29.6 Å
Structure data

EMDB-11604:
Respiratory chain supercomplex I1III2IV2 in rat heart mitochondria
Method: EM (subtomogram averaging) / Resolution: 27.7 Å

EMDB-11605:
Respiratory chain supercomplex I1III2IV1 in rat heart mitochondria
Method: EM (subtomogram averaging) / Resolution: 29.6 Å

Source
  • Rattus norvegicus (Norway rat)

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