ArticleProceedings of the National Academy of Sciences of the United States of America2021
Deactivation blocks proton pathways in the mitochondrial complex I.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
- A ratiometric fluorescent reporter of mitochondrial sodium.Nature chemical biology · 2026Article
- A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Nature communications · 2026Article
- Cavity acidification limits ferritin iron biomineralization.Journal of inorganic biochemistry · 2026Article
- Hydration-Controlled Proton Transport in Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Article
- Molecular Mechanism of Mitochondrial Complex I Disruption by m.14484T>C Underlying Leber Hereditary Optic Neuropathy.bioRxiv : the preprint server for biology · 2026Article
- Proton Transfer through a Charged Conduit in Respiratory Complex I: Long-Range Effects and Conformational Gating.Journal of chemical information and modeling · 2025Article
- A fixed mutation in the respiratory complex I impairs mitochondrial bioenergetics in the endangered Apennine brown bear.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Quinone chemistry in respiratory complex I involves protonation of a conserved aspartic acid residue.FEBS letters · 2024Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology.Antioxidants & redox signaling · 2023Review
- A New Quinone-Based Inhibitor of Mitochondrial Complex I in D-Conformation, Producing Invasion Reduction and Sensitization to Venetoclax in Breast Cancer Cells.Antioxidants (Basel, Switzerland) · 2023Article
- Quinone Catalysis Modulates Proton Transfer Reactions in the Membrane Domain of Respiratory Complex I.Journal of the American Chemical Society · 2023Article
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]-Hydrogenase Complex HydABC.Journal of the American Chemical Society · 2023Article
- From the 'black box' to 'domino effect' mechanism: what have we learned from the structures of respiratory complex I.The Biochemical journal · 2023Review
- Article
- Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?Current opinion in structural biology · 2022Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellular respiration is powered by membrane-bound redox enzymes that convert chemical energy into an electrochemical proton gradient and drive the energy metabolism. By combining large-scale classical and quantum mechanical simulations with cryo-electron microscopy data, we resolve here molecular details of conformational changes linked to proton pumping in the mammalian complex I. Our data suggest that complex I deactivation blocks water-mediated proton transfer between a membrane-bound quinone site and proton-pumping modules, decoupling the energy-transduction machinery. We identify a putative gating region at the interface between membrane domain subunits ND1 and ND3/ND4L/ND6 that modulates the proton transfer by conformational changes in transmembrane helices and bulky residues. The region is perturbed by mutations linked to human mitochondrial disorders and is suggested to also undergo conformational changes during catalysis of simpler complex I variants that lack the "active"-to-"deactive" transition. Our findings suggest that conformational changes in transmembrane helices modulate the proton transfer dynamics by wetting/dewetting transitions and provide important functional insight into the mammalian respiratory complex I.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.