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287 related items for PubMed ID: 25868873

  • 1.
    ; . PubMed ID:
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  • 2. Roles of semiquinone species in proton pumping mechanism by complex I.
    Nakamaru-Ogiso E, Narayanan M, Sakyiama JA.
    J Bioenerg Biomembr; 2014 Aug; 46(4):269-77. PubMed ID: 25077450
    [Abstract] [Full Text] [Related]

  • 3. Characterization of the delta muH+-sensitive ubisemiquinone species (SQ(Nf)) and the interaction with cluster N2: new insight into the energy-coupled electron transfer in complex I.
    Yano T, Dunham WR, Ohnishi T.
    Biochemistry; 2005 Feb 08; 44(5):1744-54. PubMed ID: 15683258
    [Abstract] [Full Text] [Related]

  • 4. Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I).
    Pohl T, Spatzal T, Aksoyoglu M, Schleicher E, Rostas AM, Lay H, Glessner U, Boudon C, Hellwig P, Weber S, Friedrich T.
    Biochim Biophys Acta; 2010 Dec 08; 1797(12):1894-900. PubMed ID: 20959113
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  • 5. EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ.
    Magnitsky S, Toulokhonova L, Yano T, Sled VD, Hägerhäll C, Grivennikova VG, Burbaev DS, Vinogradov AD, Ohnishi T.
    J Bioenerg Biomembr; 2002 Jun 08; 34(3):193-208. PubMed ID: 12171069
    [Abstract] [Full Text] [Related]

  • 6. Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.
    Narayanan M, Gabrieli DJ, Leung SA, Elguindy MM, Glaser CA, Saju N, Sinha SC, Nakamaru-Ogiso E.
    J Biol Chem; 2013 May 17; 288(20):14310-14319. PubMed ID: 23543743
    [Abstract] [Full Text] [Related]

  • 7. Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.
    Narayanan M, Sakyiama JA, Elguindy MM, Nakamaru-Ogiso E.
    J Biochem; 2016 Oct 17; 160(4):205-215. PubMed ID: 27118783
    [Abstract] [Full Text] [Related]

  • 8. Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I.
    Ohnishi T, Johnson JE, Yano T, Lobrutto R, Widger WR.
    FEBS Lett; 2005 Jan 17; 579(2):500-6. PubMed ID: 15642366
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  • 9. Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I.
    Steimle S, Willistein M, Hegger P, Janoschke M, Erhardt H, Friedrich T.
    FEBS Lett; 2012 Mar 23; 586(6):699-704. PubMed ID: 22326235
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  • 10. The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping.
    Holt PJ, Morgan DJ, Sazanov LA.
    J Biol Chem; 2003 Oct 31; 278(44):43114-20. PubMed ID: 12923180
    [Abstract] [Full Text] [Related]

  • 11. Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I.
    Steimle S, Schnick C, Burger EM, Nuber F, Krämer D, Dawitz H, Brander S, Matlosz B, Schäfer J, Maurer K, Glessner U, Friedrich T.
    Mol Microbiol; 2015 Oct 31; 98(1):151-61. PubMed ID: 26115017
    [Abstract] [Full Text] [Related]

  • 12. EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a.
    Uhlmann M, Friedrich T.
    Biochemistry; 2005 Feb 08; 44(5):1653-8. PubMed ID: 15683249
    [Abstract] [Full Text] [Related]

  • 13. Five decades of research on mitochondrial NADH-quinone oxidoreductase (complex I).
    Ohnishi T, Ohnishi ST, Salerno JC.
    Biol Chem; 2018 Oct 25; 399(11):1249-1264. PubMed ID: 30243012
    [Abstract] [Full Text] [Related]

  • 14. Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I).
    Euro L, Belevich G, Verkhovsky MI, Wikström M, Verkhovskaya M.
    Biochim Biophys Acta; 2008 Sep 25; 1777(9):1166-72. PubMed ID: 18590697
    [Abstract] [Full Text] [Related]

  • 15. Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (Complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes.
    Ohnishi T, Ohnishi ST, Shinzawa-Ito K, Yoshikawa S.
    Biofactors; 2008 Sep 25; 32(1-4):13-22. PubMed ID: 19096096
    [Abstract] [Full Text] [Related]

  • 16. Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
    Schneider D, Pohl T, Walter J, Dörner K, Kohlstädt M, Berger A, Spehr V, Friedrich T.
    Biochim Biophys Acta; 2008 Sep 25; 1777(7-8):735-9. PubMed ID: 18394423
    [Abstract] [Full Text] [Related]

  • 17. Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli.
    Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T.
    Biochim Biophys Acta; 2012 Jun 25; 1817(6):863-71. PubMed ID: 22063474
    [Abstract] [Full Text] [Related]

  • 18. Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
    Pohl T, Schneider D, Hielscher R, Stolpe S, Dörner K, Kohlstädt M, Böttcher B, Hellwig P, Friedrich T.
    Biochem Soc Trans; 2008 Oct 25; 36(Pt 5):971-5. PubMed ID: 18793172
    [Abstract] [Full Text] [Related]

  • 19. Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities.
    Torres-Bacete J, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T.
    J Biol Chem; 2007 Dec 21; 282(51):36914-22. PubMed ID: 17977822
    [Abstract] [Full Text] [Related]

  • 20. Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I.
    Baranova EA, Morgan DJ, Sazanov LA.
    J Struct Biol; 2007 Aug 21; 159(2):238-42. PubMed ID: 17360196
    [Abstract] [Full Text] [Related]

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