ArticleThe Journal of biological chemistry2009
Features of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- 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
- How inter-subunit contacts in the membrane domain of complex I affect proton transfer energetics.Biochimica et biophysica acta. Bioenergetics · 2018Article
- 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
- 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
- Article
- 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
- 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
- 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
- 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
- Tracing the trail of protons through complex I of the mitochondrial respiratory chain.PLoS biology · 2011Article
- Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.PloS one · 2011Article
- The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.The Journal of biological chemistry · 2010Article
- Transmembrane topology of subunit N of complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli.Journal of bioenergetics and biomembranes · 2010Article
- Article
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5 authors.
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Abstract
The bacterial H(+)-pumping NADH-quinone oxidoreductase (NDH-1) is an L-shaped membrane-bound enzymatic complex. Escherichia coli NDH-1 is composed of 13 subunits (NuoA-N). NuoM (ND4) subunit is one of the hydrophobic subunits that constitute the membrane arm of NDH-1 and was predicted to bear 14 helices. We attempted to clarify the membrane topology of NuoM by the introduction of histidine tags into different positions by chromosomal site-directed mutagenesis. From the data, we propose a topology model containing 12 helices (helices I-IX and XII-XIV) located in transmembrane position and two (helices X and XI) present in the cytoplasm. We reported previously that residue Glu(144) of NuoM was located in the membrane (helix V) and was essential for the energy-coupling activities of NDH-1 (Torres-Bacete, J., Nakamaru-Ogiso, E., Matsuno-Yagi, A., and Yagi, T. (2007) J. Biol. Chem. 282, 36914-36922). Using mutant E144A, we studied the effect of shifting the glutamate residue to all sites within helix V and three sites each in helix IV and VI on the function of NDH-1. Twenty double site-directed mutants including the mutation E144A were constructed and characterized. None of the mutants showed alteration in the detectable levels of expressed NuoM or on the NDH-1 assembly. In addition, most of the double mutants did not restore the energy transducing NDH-1 activities. Only two mutants E144A/F140E and E144A/L147E, one helix turn downstream and upstream restored the energy transducing activities of NDH-1. Based on these results, a role of Glu(144) for proton translocation has been discussed.
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