Nesterov Semen, Chesnokov Yury, Kamyshinsky Roman, Panteleeva Alisa, Lyamzaev Konstantin, Vasilov Raif, Yaguzhinsky Lev
Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, 123182 Moscow, Russia.
Moscow Institute of Physics and Technology, 141701 Dolgoprudny, Russia.
Int J Mol Sci. 2021 Feb 2;22(3):1462. doi: 10.3390/ijms22031462.
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.
长期以来，基于功能证据推测存在一种完整的氧化磷酸化系统（OXPHOS）超复合物，它包括电子传递系统和ATP合酶。然而，尚未获得ATP合酶与质子泵对接的结构证实。在本研究中，采用冷冻电子断层扫描技术揭示大鼠心脏线粒体嵴在ATP合成过程中的超分子结构。通过亚断层平均法确定了呼吸体和ATP合酶的原位结构。对线粒体内膜的重建结果表明，呼吸链超复合物行可与ATP合酶行对接，形成寡聚有序簇。这些有序簇表明了一种新型的OXPHOS结构组织。它应能确保OXPHOS的快速性、效率和抗损伤性，使质子沿着横向pH梯度从泵直接转移至ATP合酶，而不消耗能量。
