ArticleNature communications2024
Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.Free radical biology & medicine · 2026Review
- PCET-Inspired Nanoparticles Enable Paired Proton-Electron Delivery to Restore Mitochondrial Electron Transport and Regenerate Bone During Aging.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Nature communications · 2026Article
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Quinones operate as proton-collecting antennas in energy-transducing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Action at a distance: The remarkable coupling of COProceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The respiratory Complex I is a highly intricate redox-driven proton pump that powers oxidative phosphorylation across all domains of life. Yet, despite major efforts in recent decades, its long-range energy transduction principles remain highly debated. We create here minimal proton-conducting membrane modules by engineering and dissecting the key elements of the bacterial Complex I. By combining biophysical, biochemical, and computational experiments, we show that the isolated antiporter-like modules of Complex I comprise all functional elements required for conducting protons across proteoliposome membranes. We find that the rate of proton conduction is controlled by conformational changes of buried ion-pairs that modulate the reaction barriers by electric field effects. The proton conduction is also modulated by bulky residues along the proton channels that are key for establishing a tightly coupled proton pumping machinery in Complex I. Our findings provide direct experimental evidence that the individual antiporter modules are responsible for the proton transport activity of Complex I. On a general level, our findings highlight electrostatic and conformational coupling mechanisms in the modular energy-transduction machinery of Complex I with distinct similarities to other enzymes.
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