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• W3124996415 abstract "Complex I functions as a primary redox-driven proton pump in aerobic respiratory chains, establishing a proton motive force that powers ATP synthesis and active transport. Recent cryo-electron microscopy (cryo-EM) experiments have resolved the mammalian complex I in the biomedically relevant active (A) and deactive (D) states (Zhu et al., 2016; Fiedorczuk et al., 2016; Agip et al., 2018 [[1], [2], [3]]) that could regulate enzyme turnover, but it still remains unclear how the conformational state and activity are linked. We show here how global motion along the A/D transition accumulates molecular strain at specific coupling regions important for both redox chemistry and proton pumping. Our data suggest that the A/D motion modulates force propagation pathways between the substrate-binding site and the proton pumping machinery that could alter electrostatic and conformational coupling across large distances. Our findings provide a molecular basis to understand how global protein dynamics can modulate the biological activity of large molecular complexes." @default.
• W3124996415 created "2021-02-01" @default.
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• W3124996415 date "2021-05-01" @default.
• W3124996415 modified "2023-10-18" @default.
• W3124996415 title "Molecular strain in the active/deactive-transition modulates domain coupling in respiratory complex I" @default.
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• W3124996415 doi "https://doi.org/10.1016/j.bbabio.2021.148382" @default.
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