ArticleBiochemistry2010
Pivotal roles of three conserved carboxyl residues of the NuoC (30k) segment in the structural integrity of proton-translocating NADH-quinone oxidoreductase from Escherichia coli.
Article in Biochemistry, 2010. 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, 13 citations in OpenAlex.
- Genome-wide screening of the Keio collection identifies genetic determinants of Escherichia coli sensitivity and tolerance to benzoic acid.World journal of microbiology & biotechnology · 2026Article
- Synthetic CmBio · 2025Article
- Transcriptome Analysis Reveals the Effect of PdhR inInternational journal of molecular sciences · 2023Article
- [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
- The N-terminal domains of the paralogous HycE and NuoCD govern assembly of the respective formate hydrogenlyase and NADH dehydrogenase complexes.FEBS open bio · 2020Article
- Characterization of the Nqo5 subunit of bacterial complex I in the isolated state.FEBS open bio · 2016Article
- Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).Biochemistry · 2015Article
- Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2).The Journal of biological chemistry · 2013Article
- Roles of subunit NuoK (ND4L) in the energy-transducing mechanism of Escherichia coli NDH-1 (NADH:quinone oxidoreductase).The Journal of biological chemistry · 2012Article
- Electron transfer in subunit NuoI (TYKY) of Escherichia coli NADH:quinone oxidoreductase (NDH-1).The Journal of biological chemistry · 2012Article
- YgfZ contributes to secretion of cytotoxic necrotizing factor 1 into outer-membrane vesicles in Escherichia coli.Microbiology (Reading, England) · 2012Article
- Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.The Journal of biological chemistry · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The prokaryotic proton-translocating NADH-quinone oxidoreductase (NDH-1) is an L-shaped membrane-bound enzyme that contains 14 subunits (NuoA-NuoN or Nqo1-Nqo14). All subunits have their counterparts in the eukaryotic enzyme (complex I). NDH-1 consists of two domains: the peripheral arm (NuoB, -C, -D, -E, -F, -G, and -I) and the membrane arm (NuoA, -H, -J, -K, -L, -M, and -N). In Escherichia coli NDH-1, the hydrophilic subunits NuoC/Nqo5/30k and NuoD/Nqo4/49k are fused together in a single polypeptide as the NuoCD subunit. The NuoCD subunit is the only subunit that does not bear a cofactor in the peripheral arm. While some roles for inhibitor and quinone association have been reported for the NuoD segment, structural and functional roles of the NuoC segment remain mostly elusive. In this work, 14 highly conserved residues of the NuoC segment were mutated and 21 mutants were constructed using the chromosomal gene manipulation technique. From the enzymatic assays and immunochemical and blue-native gel analyses, it was found that residues Glu-138, Glu-140, and Asp-143 that are thought to be in the third α-helix are absolutely required for the energy-transducing NDH-1 activities and the assembly of the whole enzyme. Together with available information for the hydrophobic subunits, we propose that Glu-138, Glu-140, and Asp-143 of the NuoC segment may have a pivotal role in the structural stability of NDH-1.
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