The molecular structure of the transmembrane domain of ATP synthases is responsible for the inner mitochondrial membrane bending. According to the hypothesized mechanism, ATP synthase dissociation from dimers to monomers, triggered by Ca²⁺ binding to F₁, allows the mitochondrial permeability transition pore formation at the interface between the detached monomers.

中文翻译：

---

ATP合酶单体之间的致死通道

ATP合酶的跨膜结构域的分子结构负责内部线粒体膜的弯曲。根据假设的机制，由Ca ²⁺与F ₁结合触发的ATP合酶从二聚体解离为单体，允许线粒体通透性过渡孔在分离的单体之间的界面处形成。