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213 related items for PubMed ID: 22063474
1. 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; 1817(6):863-71. PubMed ID: 22063474 [Abstract] [Full Text] [Related]
2. 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 Jun; 1777(7-8):735-9. PubMed ID: 18394423 [Abstract] [Full Text] [Related]
3. Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I). Friedrich T, Dekovic DK, Burschel S. Biochim Biophys Acta; 2016 Mar; 1857(3):214-23. PubMed ID: 26682761 [Abstract] [Full Text] [Related]
4. 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]
5. Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Pohl T, Uhlmann M, Kaufenstein M, Friedrich T. Biochemistry; 2007 Sep 18; 46(37):10694-702. PubMed ID: 17722886 [Abstract] [Full Text] [Related]
6. 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 18; 1797(12):1894-900. PubMed ID: 20959113 [Abstract] [Full Text] [Related]
7. ErpA is important but not essential for the Fe/S cluster biogenesis of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Oppermann S, Höfflin S, Friedrich T. Biochim Biophys Acta Bioenerg; 2020 Dec 01; 1861(12):148286. PubMed ID: 32777304 [Abstract] [Full Text] [Related]
9. 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 01; 160(4):205-215. PubMed ID: 27118783 [Abstract] [Full Text] [Related]
11. A possible role for iron-sulfur cluster N2 in proton translocation by the NADH: ubiquinone oxidoreductase (complex I). Flemming D, Stolpe S, Schneider D, Hellwig P, Friedrich T. J Mol Microbiol Biotechnol; 2005 Oct 01; 10(2-4):208-22. PubMed ID: 16645316 [Abstract] [Full Text] [Related]
13. Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB. Flemming D, Schlitt A, Spehr V, Bischof T, Friedrich T. J Biol Chem; 2003 Nov 28; 278(48):47602-9. PubMed ID: 12975362 [Abstract] [Full Text] [Related]
14. Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer. Pohl T, Bauer T, Dörner K, Stolpe S, Sell P, Zocher G, Friedrich T. Biochemistry; 2007 Jun 05; 46(22):6588-96. PubMed ID: 17489563 [Abstract] [Full Text] [Related]
15. 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 05; 36(Pt 5):971-5. PubMed ID: 18793172 [Abstract] [Full Text] [Related]
16. Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I. Narayanan M, Leung SA, Inaba Y, Elguindy MM, Nakamaru-Ogiso E. Biochim Biophys Acta; 2015 Aug 05; 1847(8):681-9. PubMed ID: 25868873 [Abstract] [Full Text] [Related]
18. 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]
19. 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 17; 1777(9):1166-72. PubMed ID: 18590697 [Abstract] [Full Text] [Related]
20. Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone. Amarneh B, Vik SB. Biochemistry; 2003 May 06; 42(17):4800-8. PubMed ID: 12718520 [Abstract] [Full Text] [Related] Page: [Next] [New Search]