Cryo-electron microscopy reveals how acetogenins inhibit mitochondrial respiratory complex I.

ABSTRACT: Mitochondrial complex I (NADH:ubiquinone oxidoreductase), a crucial enzyme in energy metabolism, captures the redox potential energy from NADH oxidation/ubiquinone reduction to create the proton motive force used to drive ATP synthesis in oxidative phosphorylation. High-resolution single-particle electron cryo-EM analyses have provided detailed structural knowledge of the catalytic machinery of complex I, but not of the molecular principles of its energy transduction mechanism. Although ubiquinone is considered to bind in a long channel at the interface of the membrane-embedded and hydrophilic domains, with channel residues likely involved in coupling substrate reduction to proton translocation, no structures with the channel fully occupied have yet been described. Here, we report the stru

SUBMITTER: Grba DN 

PROVIDER: S-EPMC8861642 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature