ArticleJournal of the American Chemical Society2017
Terminal Electron-Proton Transfer Dynamics in the Quinone Reduction of Respiratory Complex I.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 82 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 carboxylate switch point controls long-range energy transduction in respiratory Complex I.Nature communications · 2026Article
- The Anionic States of Ubiquinone Characterized by Second-Order Approximate Coupled-Cluster Theory.Journal of computational chemistry · 2026Article
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Conformational Dynamics of NaJournal of chemical information and modeling · 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
- The redox driven NaNature communications · 2026Article
- Molecular Mechanism of Mitochondrial Complex I Disruption by m.14484T>C Underlying Leber Hereditary Optic Neuropathy.bioRxiv : the preprint server for biology · 2026Article
- Hydrophilic metformin and hydrophobic biguanides inhibit mitochondrial complex I by distinct mechanisms.Nature structural & molecular 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
- Molecular principles of redox-coupled sodium pumping of the ancient Rnf machinery.Nature communications · 2025Article
- Molecular Principles of Proton-Coupled Quinone Reduction in the Membrane-Bound Superoxide Oxidase.Journal of the American Chemical Society · 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
- Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2024Article
- Long-range charge transfer mechanism of the IIINature communications · 2024Article
- 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
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complex I functions as a redox-driven proton pump in aerobic respiratory chains. By reducing quinone (Q), complex I employs the free energy released in the process to thermodynamically drive proton pumping across its membrane domain. The initial Q reduction step plays a central role in activating the proton pumping machinery. In order to probe the energetics, dynamics, and molecular mechanism for the proton-coupled electron transfer process linked to the Q reduction, we employ here multiscale quantum and classical molecular simulations. We identify that both ubiquinone (UQ) and menaquinone (MQ) can form stacking and hydrogen-bonded interactions with the conserved Q-binding-site residue His-38 and that conformational changes between these binding modes modulate the Q redox potentials and the rate of electron transfer (eT) from the terminal N2 iron-sulfur center. We further observe that, while the transient formation of semiquinone is not proton-coupled, the second eT process couples to a semiconcerted proton uptake from conserved tyrosine (Tyr-87) and histidine (His-38) residues within the active site. Our calculations indicate that both UQ and MQ have low redox potentials around -260 and -230 mV, respectively, in the Q-binding site, respectively, suggesting that release of the Q toward the membrane is coupled to an energy transduction step that could thermodynamically drive proton pumping in complex I.
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