ArticlePloS one2011
Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- Quinone Catalysis Modulates Proton Transfer Reactions in the Membrane Domain of Respiratory Complex I.Journal of the American Chemical Society · 2023Article
- Horizontal proton transfer across the antiporter-like subunits in mitochondrial respiratory complex I.Chemical science · 2023Article
- Article
- Analysis of Human Clinical Mutations of Mitochondrial ND1 in a Bacterial Model System for Complex I.Life (Basel, Switzerland) · 2022Article
- Subunits E-F-G of E. coli Complex I can form an active complex when expressed alone, but in time-delayed assembly co-expression of B-CD-E-F-G is optimal.Biochimica et biophysica acta. Bioenergetics · 2022Article
- Human clinical mutations in mitochondrially encoded subunits of Complex I can be successfully modeled in E. coli.Mitochondrion · 2022Article
- Cloning and Organelle Expression of Bamboo Mitochondrial Complex I Subunits Nad1, Nad2, Nad4, and Nad5 in the YeastInternational journal of molecular sciences · 2022Article
- Paracoccus denitrificans: a genetically tractable model system for studying respiratory complex I.Scientific reports · 2021Article
- Analysis of the assembly pathway for membrane subunits of Complex I reveals that subunit L (ND5) can assemble last inBBA advances · 2021Article
- Protein Motifs for Proton Transfers That Build the Transmembrane Proton Gradient.Frontiers in chemistry · 2021Review
- Functional Water Wires Catalyze Long-Range Proton Pumping in the Mammalian Respiratory Complex I.Journal of the American Chemical Society · 2020Article
- Water-Gated Proton Transfer Dynamics in Respiratory Complex I.Journal of the American Chemical Society · 2020Article
- Role of Second Quinone Binding Site in Proton Pumping by Respiratory Complex I.Frontiers in chemistry · 2019Article
- How inter-subunit contacts in the membrane domain of complex I affect proton transfer energetics.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.Journal of the Royal Society, Interface · 2018Review
- Role of water and protein dynamics in proton pumping by respiratory complex I.Scientific reports · 2017Article
- Symmetry-related proton transfer pathways in respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Biochimica et biophysica acta · 2016Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe membrane arm of Complex I (NADH:ubiquinone oxidoreductase) contains three large, and closely related subunits, which are called L, M, and N in E. coli. These subunits are homologous to components of multi-subunit Na(+)/H(+) antiporters, and so are implicated in proton translocation. METHODOLOGY/PRINCIPAL
findingsNineteen site-specific mutations were constructed at two corresponding positions in each of the three subunits. Two positions were selected in each subunit: L_K169, M_K173, N_K158 and L_Q236, M_H241, N_H224. Membrane vesicles were prepared from all of the resulting mutant strains, and were assayed for deamino-NADH oxidase activity, proton translocation, ferricyanide reductase activity, and sensitivity to capsaicin. Corresponding mutations in the three subunits were found to have very similar effects on all activities measured. In addition, the effect of adding exogenous decylubiquinone on these activities was tested. 50 µM decylubiquinone stimulated both deamino-NADH oxidase activity and proton translocation by wild type membrane vesicles, but was inhibitory towards the same activities by membrane vesicles bearing the lysine substitution at the L236/M241/N224 positions. CONCLUSIONS/SIGNIFICANCE: The results show a close correlation with reduced activity among the corresponding mutations, and provide evidence that the L, M, and N subunits have a common role in Complex I.
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