ArticleThe Journal of biological chemistry2013
Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2).
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026Article
- Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.International journal of molecular sciences · 2026Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Cloning and Organelle Expression of Bamboo Mitochondrial Complex I Subunits Nad1, Nad2, Nad4, and Nad5 in the YeastInternational journal of molecular sciences · 2022Article
- HyfF subunit of hydrogenase 4 is crucial for regulating FJournal of bioenergetics and biomembranes · 2022Article
- Transcriptome Analysis of the Response of MatureAntibiotics (Basel, Switzerland) · 2022Article
- Molecular Dynamics Simulation of T10609C and C10676G Mutations of MitochondrialBioinformatics and biology insights · 2020Article
- Article
- Differences in the phenotypic effects of mutations in homologous MrpA and MrpD subunits of the multi-subunit Mrp-type NaExtremophiles : life under extreme conditions · 2017Article
- Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS.Journal of molecular microbiology and biotechnology · 2017Article
- Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Biochimica et biophysica acta · 2016Article
- Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.Biochimica et biophysica acta · 2016Review
- Loss of Complex I activity in the Escherichia coli enzyme results from truncating the C-terminus of subunit K, but not from cross-linking it to subunits N or L.Journal of bioenergetics and biomembranes · 2016Article
- Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.The Journal of biological chemistry · 2015Article
- Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I.Biochimica et biophysica acta · 2015Article
- A giant molecular proton pump: structure and mechanism of respiratory complex I.Nature reviews. Molecular cell biology · 2015Review
- Article
- Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).Biochemistry · 2015Article
- Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation.Journal of bioenergetics and biomembranes · 2014Review
- On the mechanism of respiratory complex I.Journal of bioenergetics and biomembranes · 2014Review
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5 authors.
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Abstract
The proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) contains a peripheral and a membrane domain. Three antiporter-like subunits in the membrane domain, NuoL, NuoM, and NuoN (ND5, ND4 and ND2, respectively), are structurally similar. We analyzed the role of NuoN in Escherichia coli NDH-1. The lysine residue at position 395 in NuoN (NLys(395)) is conserved in NuoL (LLys(399)) but is replaced by glutamic acid (MGlu(407)) in NuoM. Our mutation study on NLys(395) suggests that this residue participates in the proton translocation. Furthermore, we found that MGlu(407) is also essential and most likely interacts with conserved LArg(175). Glutamic acids, NGlu(133), MGlu(144), and LGlu(144), are corresponding residues. Unlike mutants of MGlu(144) and LGlu(144), mutation of NGlu(133) scarcely affected the energy-transducing activities. However, a double mutant of NGlu(133) and nearby KGlu(72) showed significant inhibition of these activities. This suggests that NGlu(133) bears a functional role similar to LGlu(144) and MGlu(144) but its mutation can be partially compensated by the nearby carboxyl residue. Conserved prolines located at loops of discontinuous transmembrane helices of NuoL, NuoM, and NuoN were shown to play a similar role in the energy-transducing activity. It seems likely that NuoL, NuoM, and NuoN pump protons by a similar mechanism. Our data also revealed that NLys(158) is one of the key interaction points with helix HL in NuoL. A truncation study indicated that the C-terminal amphipathic segments of NTM14 interacts with the Mβ sheet located on the opposite side of helix HL. Taken together, the mechanism of H(+) translocation in NDH-1 is discussed.
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