ArticleBiochimica et biophysica acta. Bioenergetics2018
How inter-subunit contacts in the membrane domain of complex I affect proton transfer energetics.
Article in Biochimica et biophysica acta. Bioenergetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Action at a distance: The remarkable coupling of COProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Functional Water Wires Catalyze Long-Range Proton Pumping in the Mammalian Respiratory Complex I.Journal of the American Chemical Society · 2020Article
- Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation.Nature structural & molecular biology · 2020Article
- Key role of quinone in the mechanism of respiratory complex I.Nature communications · 2020Article
- Water-Gated Proton Transfer Dynamics in Respiratory Complex I.Journal of the American Chemical Society · 2020Article
- Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I.Nature communications · 2020Article
- Electric field modulated redox-driven protonation and hydration energetics in energy converting enzymes.Chemical communications (Cambridge, England) · 2019Article
- Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019Article
- How cardiolipin modulates the dynamics of respiratory complex I.Science advances · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The respiratory complex I is a redox-driven proton pump that employs the free energy released from quinone reduction to pump protons across its complete ca. 200 Å wide membrane domain. Despite recently resolved structures and molecular simulations, the exact mechanism for the proton transport process remains unclear. Here we combine large-scale molecular simulations with quantum chemical density functional theory (DFT) models to study how contacts between neighboring antiporter-like subunits in the membrane domain of complex I affect the proton transfer energetics. Our combined results suggest that opening of conserved Lys/Glu ion pairs within each antiporter-like subunit modulates the barrier for the lateral proton transfer reactions. Our work provides a mechanistic suggestion for key coupling effects in the long-range force propagation process of complex I.
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