T Friedrich

Summary

Affiliation: University of Freiburg
Country: Germany

Publications

  1. ncbi request reprint Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut für Org Chemie und Biochemie, Albert Ludwigs Universitat, Albertstr 21, D 79104 Freiburg, Germany
    Biochem Soc Trans 33:836-9. 2005
  2. ncbi request reprint The gross structure of the respiratory complex I: a Lego System
    Thorsten Friedrich
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstr 21, D 79104 Freiburg, Germany
    Biochim Biophys Acta 1608:1-9. 2004
  3. doi request reprint Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Daniel Schneider
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstr 21, 79104 Freiburg, Germany
    Biochim Biophys Acta 1777:735-9. 2008
  4. ncbi request reprint The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
    Stefan Stolpe
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, D 79104 Freiburg, Germany
    J Biol Chem 279:18377-83. 2004
  5. ncbi request reprint EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a
    Mareike Uhlmann
    Albert Ludwigs Universitat Freiburg, Institut fur Organische Chemie und Biochemie, Albertstrasse 21, Chemiehochhaus, D 79104 Freiburg im Breisgau, Germany
    Biochemistry 44:1653-8. 2005
  6. ncbi request reprint A possible role for iron-sulfur cluster N2 in proton translocation by the NADH: ubiquinone oxidoreductase (complex I)
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Freiburg, Germany
    J Mol Microbiol Biotechnol 10:208-22. 2005
  7. ncbi request reprint Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer
    Thomas Pohl
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, Chemiehochhaus, D 79104 Freiburg i Br, Germany
    Biochemistry 46:6588-96. 2007
  8. doi request reprint Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Thomas Pohl
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat, Albertstrasse 21, D 79104 Freiburg, Germany
    Biochem Soc Trans 36:971-5. 2008
  9. ncbi request reprint Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universität Albertstr 21, 79104 Freiburg, Germany
    J Biol Chem 278:47602-9. 2003
  10. ncbi request reprint Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, D 79104 Freiburg, Germany
    J Biol Chem 281:24781-9. 2006

Collaborators

  • Thomas Pohl
  • D Schneider
  • P Hellwig
  • Werner J H Koopman
  • Ulrich Schulte
  • C Hunte
  • Matthias Boll
  • Chang-An Yu
  • Thorsten Koslowski
  • Toni Gabaldón
  • Martijn A Huynen
  • Dirk Flemming
  • Stefan Stolpe
  • Dierk Scheide
  • Jörg Johannes
  • Marius Mihasan
  • Robert Winkler
  • Ruth Hielscher
  • Raija Boll
  • Brigitte Boxma
  • Mareike Uhlmann
  • Henrik Möbitz
  • Marion Gurrath
  • Xing Gong
  • Micaela Hesterberg
  • Margarida Duarte
  • Bettina Bottcher
  • Mihaela Carmen Unciuleac
  • Eberhard Warkentin
  • Uli Ermler
  • Ingrid Richter
  • Christian Hertweck
  • Vlad Artenie
  • Calin Bogdan Chiribau
  • Georg Zocher
  • Georg E Schulz
  • Roderich Brandsch
  • Tina Wenz
  • Steffen Glaser
  • Andreas Bechthold
  • Daniel P Kloer
  • Carsten Hofmann
  • Simone Lepper
  • Björn Heitmann
  • Gerd Hauser
  • Rob M de Graaf
  • Johannes H P Hackstein
  • Marten Veenhuis
  • Seung Yeo Moon-van der Staay
  • Georg W M van der Staay
  • Angela H A M van Hoek
  • Theo A van Alen
  • Guenola Ricard
  • Aloysius G M Tielens
  • Jaap J van Hellemond
  • Linda Yu
  • Tong Xie
  • Tobias Bischof
  • Volker Spehr
  • Angela Schlitt
  • Robert Huber
  • Helena Pópulo
  • Luitgard Nagel-Steger
  • Arnaldo Videira

Detail Information

Publications27

  1. ncbi request reprint Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut für Org Chemie und Biochemie, Albert Ludwigs Universitat, Albertstr 21, D 79104 Freiburg, Germany
    Biochem Soc Trans 33:836-9. 2005
    ..We did not find any indications for Na+ translocation by the E. coli complex I...
  2. ncbi request reprint The gross structure of the respiratory complex I: a Lego System
    Thorsten Friedrich
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstr 21, D 79104 Freiburg, Germany
    Biochim Biophys Acta 1608:1-9. 2004
    ..This model reflects the evolution of complex I from pre-existing modules for electron transfer and proton translocation...
  3. doi request reprint Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Daniel Schneider
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstr 21, 79104 Freiburg, Germany
    Biochim Biophys Acta 1777:735-9. 2008
    ..It is discussed whether this fragment represents an assembly intermediate. In addition, a membrane-bound fragment exhibiting NADH/ferricyanide oxidoreductase activity and containing the iron-sulfur cluster N2 was detected in one mutant...
  4. ncbi request reprint The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport
    Stefan Stolpe
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, D 79104 Freiburg, Germany
    J Biol Chem 279:18377-83. 2004
    ..coli complex I is a primary electrogenic proton pump. However, the magnitude of the pH gradient depended on the sodium concentration. The capability of complex I for secondary Na(+)/H(+) antiport is discussed...
  5. ncbi request reprint EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a
    Mareike Uhlmann
    Albert Ludwigs Universitat Freiburg, Institut fur Organische Chemie und Biochemie, Albertstrasse 21, Chemiehochhaus, D 79104 Freiburg im Breisgau, Germany
    Biochemistry 44:1653-8. 2005
    ..Thus, there is no third binuclear iron-sulfur "N1c" in the E. coli complex I but an additional tetranuclear cluster that may be coined N7...
  6. ncbi request reprint A possible role for iron-sulfur cluster N2 in proton translocation by the NADH: ubiquinone oxidoreductase (complex I)
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Freiburg, Germany
    J Mol Microbiol Biotechnol 10:208-22. 2005
    ..The enzyme catalytic activity depends on the presence of cluster N2 and is coupled with major conformational changes. From these data a model for redox-induced conformation-driven proton translocation has been derived...
  7. ncbi request reprint Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer
    Thomas Pohl
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, Chemiehochhaus, D 79104 Freiburg i Br, Germany
    Biochemistry 46:6588-96. 2007
    ..Cluster N7 was detectable in the latter mutants but with shifted g-values, indicating a different ligation of N7. Thus, N7 is essential for the stability of the complex but is not involved in electron transfer...
  8. doi request reprint Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Thomas Pohl
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat, Albertstrasse 21, D 79104 Freiburg, Germany
    Biochem Soc Trans 36:971-5. 2008
    ..EPR spectroscopy of surface mutants of the complex containing a covalently bound spin label at distinct positions demonstrates NADH-dependent conformational changes in both arms of the complex...
  9. ncbi request reprint Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universität Albertstr 21, 79104 Freiburg, Germany
    J Biol Chem 278:47602-9. 2003
    ..N2 was also detected in the complex isolated from the mutant NuoI C102A. From this we conclude that the Fe/S cluster N2 is located on subunit NuoB...
  10. ncbi request reprint Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Dirk Flemming
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, D 79104 Freiburg, Germany
    J Biol Chem 281:24781-9. 2006
    ..We discuss the possible participation of Glu(67) in a proton pathway coupled with the redox reaction of N2...
  11. pmc Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH:ubiquinone oxidoreductase
    Thomas Pohl
    Institute of Organic Chemistry and Biochemistry, University of Freiburg, Freiburg, Germany
    BMC Biochem 8:13. 2007
    ..It was not clear whether frataxin is in general a component of complex I from bacteria. The Escherichia coli homologue of frataxin is coined CyaY...
  12. ncbi request reprint Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Thomas Pohl
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat, Albertstrasse 21, Spemann Graduate School of Biology and Medicine, D 79104 Freiburg i Br, Germany
    Biochemistry 46:10694-702. 2007
    ..After reconstitution in proteoliposomes it couples the electron transfer with proton translocation in an inhibitor sensitive manner, thus meeting all prerequisites for structural and functional studies...
  13. doi request reprint Redox-induced conformational changes within the Escherichia coli NADH ubiquinone oxidoreductase (complex I): an analysis by mutagenesis and FT-IR spectroscopy
    Thorsten Friedrich
    Institut fur Organische Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstr 21, 79104 Freiburg, Germany
    Biochim Biophys Acta 1797:659-63. 2010
    ..This residue is located in the vicinity of the cluster N2. Re-evaluating these previous data we here discuss a mechanism, by which the redox reaction of N2 induces conformational changes possibly leading to proton translocation...
  14. ncbi request reprint Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase
    Dirk Flemming
    Institut für Org Chemie und Biochemie, Albert Ludwigs Universitat Freiburg, Albertstrasse 21, D 79104 Freiburg, Germany
    J Biol Chem 278:3055-62. 2003
    ..Therefore, we propose that tyrosines 114 and 139 on NuoB were protonated upon reduction of cluster N2 and were thus involved in the proton-transfer reaction coupled with its redox reaction...
  15. ncbi request reprint The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli
    Xing Gong
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078, USA
    J Biol Chem 278:25731-7. 2003
    ..Using the PHDhtm hydropathy plot, the labeled peptide is located in the transmembrane helix 4 toward the periplasmic side of the membrane...
  16. ncbi request reprint Monitoring redox-dependent contribution of lipids in Fourier transform infrared difference spectra of complex I from Escherichia coli
    Ruth Hielscher
    Institut fur Biophysik, Johann Wolfgang Goethe Universitat, Max von Laue Strasse 1, D 60438 Frankfurt am Main, Germany
    Biopolymers 82:291-4. 2006
    ....
  17. ncbi request reprint The active conformation of avilamycin A is conferred by AviX12, a radical AdoMet enzyme
    Raija Boll
    Institut für Pharmazeutische Wissenschaften, Pharmazeutische Biologie und Biotechnologie, Albert Ludwigs Universitat Freiburg, Stefan Meier Strasse 19, D 79104 Freiburg, Germany
    J Biol Chem 281:14756-63. 2006
    ..The iron sulfur cluster [Fe-S] present in radical AdoMet enzymes was detected in purified AviX12 by means of electron paramagnetic resonance spectroscopy...
  18. ncbi request reprint A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    Bettina Bottcher
    Structural Biology and Biocomputing Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, D 69117 Heidelberg, Germany
    J Biol Chem 277:17970-7. 2002
    ..Only the horseshoe-shaped complex I exhibits enzyme activity in detergent solution, which is abolished by the addition of salt. Therefore, it is proposed that this structure is the native conformation of the complex in the membrane...
  19. ncbi request reprint Fourier transform infrared spectroscopic study on the conformational reorganization in Escherichia coli complex I due to redox-driven proton translocation
    Petra Hellwig
    Institut fur Biophysik, Johann Wolfgang Goethe Universitat, Theodor Stern Kai 7, Haus 75, 60590 Frankfurt M, Germany
    Biopolymers 74:69-72. 2004
    ..The amplitude of the signal is pH dependent, as expected for an energy coupling step in the enzymes reaction. Furthermore, pH-dependent protonation events and quinone binding were detected...
  20. pmc Disruption of iron-sulphur cluster N2 from NADH: ubiquinone oxidoreductase by site-directed mutagenesis
    Margarida Duarte
    Instituto de Biologia Molecular e Celular, Rua do Campo Alegre 823, 4150 180 Porto, Portugal
    Biochem J 364:833-9. 2002
    ..3 kDa protein. We also observed an interference with the reduction of redox group X, suggesting that cluster N2 is the electron donor to this high-potential redox group...
  21. ncbi request reprint Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes
    Henrik Möbitz
    Institut fur Biologie II, Mikrobiologie, Universitat Freiburg, Schanzlestrasse 1, D 79104 Freiburg, Germany
    Biochemistry 43:1376-85. 2004
    ..Implications for the overall catalytic cycle of benzoyl-CoA reductase are discussed and compared with other ATP-hydrolyzing enzymes...
  22. doi request reprint Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase
    Jörg Johannes
    Institute of Biochemistry, University of Leipzig, D 04103 Leipzig, Germany
    Biochemistry 47:4964-72. 2008
    ..Both dithionite and azide bound directly to equatorial ligation sites of the Mo atom. The results obtained revealed further insights into the active site of an unusual member of the XO family of molybdenum cofactor containing enzymes...
  23. ncbi request reprint A binuclear manganese cluster that catalyzes radical-mediated N-oxygenation
    Robert Winkler
    Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology HKI, Beutenbergstrasse 11a, 07745 Jena, Germany
    Angew Chem Int Ed Engl 46:8605-8. 2007
  24. ncbi request reprint An anaerobic mitochondrion that produces hydrogen
    Brigitte Boxma
    Department of Evolutionary Microbiology, Faculty of Science, Radboud University Nijmegen, Toernooiveld 1, NL 6525 ED Nijmegen, The Netherlands
    Nature 434:74-9. 2005
    ..ovalis organelle as a missing link between mitochondria and hydrogenosomes...
  25. pmc An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism
    Marius Mihasan
    Institute of Biochemistry and Molecular Biology, Hermann Herder Str 7, 79104 Freiburg, Germany
    Appl Environ Microbiol 73:2479-85. 2007
    ..The NAD(P)H-nicotine blue oxidoreductase may prevent intracellular one-electron reductions of nicotine blue which may lead to semiquinone radicals and potentially toxic reactive oxygen species...
  26. ncbi request reprint Adjacent cysteines are capable of ligating the same tetranuclear iron-sulfur cluster
    Marion Gurrath
    Institut fur Pharmazeutische Chemie, Universitat Dusseldorf, Dusseldorf, Germany
    Proteins 56:556-63. 2004
    ..Thus, a slight main-chain conformational change would allow two adjacent cysteines to coordinate a [4Fe/4S] cluster...
  27. ncbi request reprint The proton-pumping NADH:ubiquinone oxidoreductase (complex I) of Aquifex aeolicus
    Dierk Scheide
    Heinrich Heine Universitat Dusseldorf, Institut fur Biochemie, Universitatsstr 1, D 40225, Dusseldorf, Germany
    FEBS Lett 512:80-4. 2002
    ..aeolicus membranes sedimented as a protein with a molecular mass of approximately 550 kDa. From the data we concluded that A. aeolicus contains a NADH:ubiquinone oxidoreductase resembling complex I of mesophilic bacteria...