ArticleProceedings of the National Academy of Sciences of the United States of America2017
Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 101 citations in OpenAlex.
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- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
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- Coenzyme Q10 trapping in mitochondrial complex I underlies Leber's hereditary optic neuropathy.Proceedings of the National Academy of Sciences of the United States of America · 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
- Using light scattering to assess how phospholipid-protein interactions affect complex I functionality in liposomes.RSC chemical biology · 2023Article
- Identification of 2-Aryl-Quinolone Inhibitors of CytochromeACS infectious diseases · 2023Article
- Structural basis of mammalian respiratory complex I inhibition by medicinal biguanides.Science (New York, N.Y.) · 2023Article
- Single protonation of the reduced quinone in respiratory complex I drives four-proton pumping.FEBS letters · 2023Article
- NDUFS3 knockout cancer cells and molecular docking reveal specificity and mode of action of anti-cancer respiratory complex I inhibitors.Open biology · 2022Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Respiratory complex I (NADH:ubiquinone oxidoreductase), one of the largest membrane-bound enzymes in mammalian cells, powers ATP synthesis by using the energy from electron transfer from NADH to ubiquinone-10 to drive protons across the energy-transducing mitochondrial inner membrane. Ubiquinone-10 is extremely hydrophobic, but in complex I the binding site for its redox-active quinone headgroup is ∼20 Å above the membrane surface. Structural data suggest it accesses the site by a narrow channel, long enough to accommodate almost all of its ∼50-Å isoprenoid chain. However, how ubiquinone/ubiquinol exchange occurs on catalytically relevant timescales, and whether binding/dissociation events are involved in coupling electron transfer to proton translocation, are unknown. Here, we use proteoliposomes containing complex I, together with a quinol oxidase, to determine the kinetics of complex I catalysis with ubiquinones of varying isoprenoid chain length, from 1 to 10 units. We interpret our results using structural data, which show the hydrophobic channel is interrupted by a highly charged region at isoprenoids 4-7. We demonstrate that ubiquinol-10 dissociation is not rate determining and deduce that ubiquinone-10 has both the highest binding affinity and the fastest binding rate. We propose that the charged region and chain directionality assist product dissociation, and that isoprenoid stepping ensures short transit times. These properties of the channel do not benefit the exhange of short-chain quinones, for which product dissociation may become rate limiting. Thus, we discuss how the long channel does not hinder catalysis under physiological conditions and the possible roles of ubiquinone/ubiquinol binding/dissociation in energy conversion.
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