ArticleThe Journal of biological chemistry2010
The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57 citing papers in PubMed, 92 citations in OpenAlex.
- Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026Article
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Directed mutagenesis of large multi-subunit protein complexes by plasmid sub-fragmentation.Scientific reports · 2026Article
- Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.Nature communications · 2026Article
- Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.International journal of molecular sciences · 2026Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- Asgard archaea modulate potential methanogenesis substrates in wetland soil.Nature communications · 2024Article
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- Horizontal proton transfer across the antiporter-like subunits in mitochondrial respiratory complex I.Chemical science · 2023Article
- Single protonation of the reduced quinone in respiratory complex I drives four-proton pumping.FEBS letters · 2023Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Structure of respiratory complex I - An emerging blueprint for the mechanism.Current opinion in structural biology · 2022Review
- Cyclic Electron Flow-Coupled Proton Pumping inMicroorganisms · 2022Article
- Cloning and Organelle Expression of Bamboo Mitochondrial Complex I Subunits Nad1, Nad2, Nad4, and Nad5 in the YeastInternational journal of molecular sciences · 2022Article
- Resolving Chemical Dynamics in Biological Energy Conversion: Long-Range Proton-Coupled Electron Transfer in Respiratory Complex I.Accounts of chemical research · 2021Article
- Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli 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
- [Mitochondrial G12630A variation is associated with statin-induced myalgia in Chinese patients with coronary artery disease].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2020Article
- Water-Gated Proton Transfer Dynamics in Respiratory Complex I.Journal of the American Chemical Society · 2020Article
- Molecular Dynamics Simulation of T10609C and C10676G Mutations of MitochondrialBioinformatics and biology insights · 2020Article
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6 authors at 3 institutions in 1 country.
Funding
Abstract
Complex I pumps protons across the membrane by using downhill redox energy. Here, to investigate the proton pumping mechanism by complex I, we focused on the largest transmembrane subunit NuoL (Escherichia coli ND5 homolog). NuoL/ND5 is believed to have H(+) translocation site(s), because of a high sequence similarity to multi-subunit Na(+)/H(+) antiporters. We mutated thirteen highly conserved residues between NuoL/ND5 and MrpA of Na(+)/H(+) antiporters in the chromosomal nuoL gene. The dNADH oxidase activities in mutant membranes were mostly at the control level or modestly reduced, except mutants of Glu-144, Lys-229, and Lys-399. In contrast, the peripheral dNADH-K(3)Fe(CN)(6) reductase activities basically remained unchanged in all the NuoL mutants, suggesting that the peripheral arm of complex I was not affected by point mutations in NuoL. The proton pumping efficiency (the ratio of H(+)/e(-)), however, was decreased in most NuoL mutants by 30-50%, while the IC(50) values for asimicin (a potent complex I inhibitor) remained unchanged. This suggests that the H(+)/e(-) stoichiometry has changed from 4H(+)/2e(-) to 3H(+) or 2H(+)/2e(-) without affecting the direct coupling site. Furthermore, 50 μm of 5-(N-ethyl-N-isopropyl)-amiloride (EIPA), a specific inhibitor for Na(+)/H(+) antiporters, caused a 38 ± 5% decrease in the initial H(+) pump activity in the wild type, while no change was observed in D178N, D303A, and D400A mutants where the H(+) pumping efficiency had already been significantly decreased. The electron transfer activities were basically unaffected by EIPA in both control and mutants. Taken together, our data strongly indicate that the NuoL subunit is involved in the indirect coupling mechanism.
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