T Friedrich

Summary

Affiliation: Heinrich Heine University
Country: Germany

Publications

  1. ncbi request reprint The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    T Friedrich
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    FEBS Lett 479:1-5. 2000
  2. ncbi request reprint Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Universitätsstrasse, Germany
    Biochim Biophys Acta 1459:305-9. 2000
  3. ncbi request reprint Redox components and structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Germany
    Biochim Biophys Acta 1365:215-9. 1998
  4. ncbi request reprint The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Universitatsstr 1, D 40225 Dusseldorf, Germany
    Biochim Biophys Acta 1364:134-46. 1998
  5. ncbi request reprint Complex I: a chimaera of a redox and conformation-driven proton pump?
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Germany
    J Bioenerg Biomembr 33:169-77. 2001
  6. ncbi request reprint Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules
    T Friedrich
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    J Theor Biol 187:529-40. 1997
  7. ncbi request reprint Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli
    H Leif
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    Eur J Biochem 230:538-48. 1995
  8. ncbi request reprint Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I)
    V Spehr
    Institut fur Biochemie, Heinrich Heine Universitat, Dusseldorf, Germany
    Biochemistry 38:16261-7. 1999
  9. ncbi request reprint Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Heinrich Heine Universitat Dusseldorf, Institut fur Biochemie, Germany
    J Bioenerg Biomembr 25:331-7. 1993
  10. ncbi request reprint The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    U Weidner
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Federal Republic of Germany
    J Mol Biol 233:109-22. 1993

Collaborators

Detail Information

Publications23

  1. ncbi request reprint The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    T Friedrich
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    FEBS Lett 479:1-5. 2000
    ..Six of them are also present in a family of membrane-bound multisubunit [NiFe] hydrogenases. It is discussed that they build a module for electron transfer coupled to proton translocation...
  2. ncbi request reprint Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Universitätsstrasse, Germany
    Biochim Biophys Acta 1459:305-9. 2000
    ..Electrochemical titration of this absorption reveals a midpoint potential of -80 mV. This group is believed to transfer electrons from the high potential FeS cluster to ubiquinone...
  3. ncbi request reprint Redox components and structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Germany
    Biochim Biophys Acta 1365:215-9. 1998
    ..Due to its positive midpoint potential the novel group is believed to transfer electrons from the FeS clusters to ubiquinone. Its role in proton translocation is discussed...
  4. ncbi request reprint The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Universitatsstr 1, D 40225 Dusseldorf, Germany
    Biochim Biophys Acta 1364:134-46. 1998
  5. ncbi request reprint Complex I: a chimaera of a redox and conformation-driven proton pump?
    T Friedrich
    Institut fur Biochemie, Universitat Dusseldorf, Germany
    J Bioenerg Biomembr 33:169-77. 2001
    ..This implies that complex I contains two energy-coupling sites. The NADH dehydrogenase module seems to be involved in electron transfer and not in proton translocation...
  6. ncbi request reprint Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules
    T Friedrich
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    J Theor Biol 187:529-40. 1997
    ..Homologues of the functional modules of the complex are also found in other bacterial electron transfer and ion transport proteins. The modular evolution of the complex and the possible origin of its modules are discussed in this paper...
  7. ncbi request reprint Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli
    H Leif
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    Eur J Biochem 230:538-48. 1995
    ..This subunit arrangement coincidences to some extent with the order of the genes on the nuo operon. A topological model of the E. coli complex I is proposed...
  8. ncbi request reprint Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I)
    V Spehr
    Institut fur Biochemie, Heinrich Heine Universitat, Dusseldorf, Germany
    Biochemistry 38:16261-7. 1999
    ..Due to its stability over a wide pH range and at very high salt concentrations, this preparation is well suited for structural investigations...
  9. ncbi request reprint Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I)
    T Friedrich
    Heinrich Heine Universitat Dusseldorf, Institut fur Biochemie, Germany
    J Bioenerg Biomembr 25:331-7. 1993
    ..This assumption is further supported by the conserved order of bacterial complex I genes, which correlates with the topological arrangement of the corresponding subunits in the two parts of complex I...
  10. ncbi request reprint The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    U Weidner
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Federal Republic of Germany
    J Mol Biol 233:109-22. 1993
    ..To some extent, the gene order correlates with the topological arrangement of the encoded subunits. The conception of modular evolution of NADH: ubiquinone oxidoreductase is further supported by the arrangement of the nuo-genes...
  11. ncbi request reprint One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography
    S Bungert
    Heinrich Heine Universitat Dusseldorf, Institut fur Biochemie, Universitatsstr 1, D 40225, Dusseldorf, Germany
    FEBS Lett 460:207-11. 1999
    ..This was achieved by fusing the Strep-tag II peptide to the C-terminus of NuoF or NuoG. Fusion of this peptide to the N-terminus of either NuoE or NuoF disturbed the assembly of the NADH dehydrogenase fragment...
  12. ncbi request reprint Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    M Braun
    Institut fur Biochemie, Heinrich Heine Universitat, Dusseldorf, Germany
    Biochemistry 37:1861-7. 1998
    ..The preparation fulfills all prerequisites for crystallization of the fragment...
  13. ncbi request reprint Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I
    H Leif
    Institute fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    Biochem Soc Trans 21:998-1001. 1993
  14. ncbi request reprint Search for novel redox groups in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy
    U Schulte
    Institut fur Biochemie, Heinrich Heine Universitat Dusseldorf, Germany
    Biofactors 8:177-86. 1998
    ..The existence of two novel groups is postulated and their possible locations in the electron pathway and their roles in proton translocation are discussed...
  15. ncbi request reprint Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I)
    T Rasmussen
    Institut fur Biochemie, Heinrich Heine Universitat, Universitatsstrasse 1, 40225 Dusseldorf, Germany
    Biochemistry 40:6124-31. 2001
    ..We detected EPR signals in a fragment of complex I which we attribute to the novel FeS clusters of complex I...
  16. ncbi request reprint A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex
    U Schulte
    Institut fur Biochemie, Heinrich Heine Universitat, Dusseldorf, Germany
    J Mol Biol 292:569-80. 1999
    ..We propose that the reductase/isomerase subunit with its NADPH cofactor takes part in the biosynthesis of this new redox group...
  17. ncbi request reprint Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase
    A Jeltsch
    Institut fur Biochemie, Fachbereich Biologie, Heinrich Buff Ring 58, Giessen, 35392, Germany
    J Mol Biol 285:1121-30. 1999
    ..The S229A variant can better flip modified bases but does not tightly lock the flipped base into the adenine-binding pocket, suggesting that Ser229 could form a contact to the flipped adenine...
  18. ncbi request reprint Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    V Guenebaut
    Structural Biology and Biocomputing Programme, European Molecular Biology Laboratory, Heidelberg, Germany
    J Mol Biol 276:105-12. 1998
    ....
  19. 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...
  20. ncbi request reprint Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide
    H C Barker
    Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, UK
    Mol Microbiol 35:1518-29. 2000
    ..Additionally, protective quantities of formate are secreted by E. coli and Salmonella during growth suggesting that such compounds are important determinants of bacterial survival in the host...
  21. ncbi request reprint Quinone-annonaceous acetogenins: synthesis and complex I inhibition studies of a new class of natural product hybrids
    S Arndt
    , , Germany
    Chemistry 7:993-1005. 2001
    ....
  22. pmc The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behavior
    S Geibel
    , D-60596 Frankfurt am Main, Germany
    Biophys J 81:2059-68. 2001
    ..From the results we conclude that the transport cycle of bR branches via a long-lived M(1)* in a voltage-dependent manner into a nontransporting cycle, where the proton release and uptake occur on the extracellular side...
  23. ncbi request reprint Structural and energetic determinants for enantiopreferences in kinetic resolution of lipases
    M Bocola
    Institute of Pharmaceutical Chemistry, University of Marburg, Marbacher Weg 6, Germany
    Protein Eng 16:319-22. 2003