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Institute of Organic Chemistry and Biochemistry
 
Faculty of Chemistry, Pharmacy
and Earth Sciences
 
University of Freiburg

 

 
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Publications

The following works by the group Prof. Friedrich were published in the last years:



The list of publications can be downloaded here. (PDF-file)

  • Morina, K., Schulte, M., Hubrich, F., Dörner, K., Steimle, S., Stolpe, S. & Friedrich, T. (2011) Engineering the Respiratory Complex I to Energy-converting NADPH:Ubiquinone Oxidoreductase. J. Biol. Chem., 286, 34627-34634.

  • Steimle, S., Bajzath, C., Dörner, K., Schulte, M., Bothe, V. & Friedrich, T. (2011) Role of Subunit NuoL for Proton Translocation by Respiratory Complex I. Biochemistry, 50, 3386-3393.

  • Pohl, T., Spatzal, T., Aksoyoglu, M., Schleicher, E., Rostas, A.M., Lay, H., Glessner, U., Boudon, C., Hellwig, P., Weber, S. & Friedrich, T. (2010) Spin labeling of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta, 1797, 1894-1900.

  • Friedrich, T. & Hellwig P. (2010) Redox-induced conformational changes within the Escherichia coli NADH:ubiquinone oxidoreductase (complex I): an analysis by mutagenesis and FT-IR spectroscopy. Biochim. Biophys. Acta, 1797, 659-663.

  • Wittekindt, C., Schwarz, M., Friedrich, T. & Koslowski, T. (2009) Aromatic Acids as Stepping Stones in Charge Transfer in Respiratory Complex I: An Unusual Mechanism Deduced from Atomistic Theory and Bioinformatics, J. Am. Chem. Soc., 131, 8134-8140.

  • Kohlstädt, M., Dörner, K., Labatzke, R., Koç, C., Hielscher, R., Schiltz, E., Einsle, O., Hellwig, P. & Friedrich, T. (2008) Heterologous Production, Isolation, Characterization and Crystallization of a Soluble Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) from Aquifex aeolicus, Biochemistry, 47, 13036-13045.

  • Pohl, T., Schneider, D., Hielscher, R., Stolpe, S., Dörner, K., Kohlstädt, M., Böttcher, B., Hellwig, P. & Friedrich, T. (2008) Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I), Biochem. Soc. Trans., 36, 971-975.

  • Schneider, D., Pohl, T., Walter, J., Dörner, K., Kohlstädt, M., Berger, A., Spehr, V. & Friedrich, T. (2008) Assembly of the Escherichia coli complex I, Biochim. Biophys. Acta, 1777, 735-739.

  • Johannes, J., Unciuleac, M-C., Friedrich, T., Warkentin, E., Ermler, U. & Boll, M. (2008) Inhibitors of Molybdenum Cofactor Containing 4-Hydroxybenzoyl-CoA Reductase.
    Biochemistry 47, 4964-4972.

  • Winkler, R., Zocher, G., Richter, I., Friedrich, T., Schulz, G.E. & Hertweck, C. (2007) A Binuclear Manganese Cluster catalyzing Radical-Mediated N-Oxygenation.
    Angew. Chem. Int. Ed. 46, 8605-8608.

  • Pohl, T., Uhlmann, M., Kaufenstein, M. & Friedrich, T. (2007) Lambda Red-Mediated Mutagenesis and Efficient Large Scale Affinity Purification of the Escherichia coli NADH:Ubiquinone Oxidoreductase (complex I).
    Biochemistry 46, 10694-10702.

  • Pohl, T., Walter, J., Stolpe, S., Defeu Soufo, H.J., Graumann, P.L. & Friedrich, T. (2007) Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH:ubiquinone oxidoreductase.
    BMC Biochemistry 8:13.

  • Pohl, T., Bauer, T., Dörner, K., Stolpe, S., Sell, P., Zocher, G. & Friedrich, T. (2007) Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer.
    Biochemistry 46, 6588-6596.

  • Mihasan, M., Chiribau, C.B., Friedrich, T., Artenie, V. & Brandsch, R. (2007) A NAD(H)P-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism.
    Appl. Environ. Microbiol. 73, 2479-2485.

  • Flemming, D., Hellwig, P., Lepper, S., Kloer, D.P. & Friedrich, T. (2006) Catalytic Importance of Acidic Amino Acids on Subunit NuoB of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I).
    J. Biol. Chem. 281, 24781-24789.

  • Boll, R., Hofmann, C., Heitmann, B., Hauser, G., Glaser, S., Koslowski, T., Friedrich, T. & Bechthold, A. (2006) The Active Conformation of Avilamycin A is Confered by AviX12, a Radical SAM Enzyme. J. Biol. Chem. 281, 14756-14763.

  • Hielscher, R., Wenz, T., Stolpe, S., Hunte, C., Friedrich, T. & Hellwig, P. (2006) Monitoring redox dependent contribution of lipids in FTIR difference spectra of complex I from E. coli. Biopolymers 82, 291-294.

  • Flemming, D., Stolpe, S., Schneider, D., Hellwig, P. & Friedrich, T. (2005) A possible role for Iron-Sulfur Cluster N2 in Proton Translocation by the NADH:Ubiquinone Oxidoreductase (Complex I). J. Mol. Microbiol. Biotech. 10, 208-220.

  • Utz, N., Engel, L., Friedrich, T. & Koslowski, T. (2005) A variational approach to protein charge transfer. Z. Phys. Chem. 219, 1391-1410.

  • Flemming, D. & Friedrich, T. (2005) Die modulare Evolution eines Enzymkomplexes. Bioforum 6/2005. Klicken sie hier , um sich den Artikel als PDF-Datei anzuschauen.

  • Friedrich, T., Stolpe, S., Schneider, D., Barquera, B. & Hellwig, P. (2005) Ion translocation by the Escherichia Coli NADH:ubiquinone oxidoreductase (complex I). Biochem. Soc. Trans 33, 836-839.

  • Boxma, B., de Graaf, R.M., van der Staay, G.W.M., van Alen, T.A., Ricard, G., Gabaldon, T., van Hoek, A.H.A.M., Moon-van der Stay, S.Y., Koopman, W.J.H., van Hellemond, J.J., Tielens, A.G.M., Friedrich, T., Veenhuis, M., Huynen, M.A. & Hackstein, J.H.P. (2005) An anaerobic mitochondrion that produces hydrogen. Nature 343, 74-79.

  • Uhlmann, M. & Friedrich, T. (2005) The EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a. Biochemistry 44, 1653-1658.

  • Gurrath, M. & Friedrich, T. (2004) Adjacent Cysteines are Capable of Ligating the Same Tetranuclear Iron-sulfur Cluster. Proteins: Structure, Function, and Bioinformatics 56, 556-563.

  • Hellwig, P., Stolpe, S. & Friedrich, T. (2004) FTIR spectroscopic study on the conformational reorganisation in E. coli complex I due to redox-driven proton translocation. Biopolymers 74, 69-72.

  • Stolpe, S. & Friedrich, T. (2004) The NADH:ubiquinone oxidoreductase of Escherichia coli is a primary proton-pump capable of secondary proton/sodium antiport. J. Biol. Chem. 279, 18377-18383.

  • Möbitz, H., Friedrich, T. & Boll, M. (2004) Substrate Binding and Reduction of Benzoyl-CoA Reductase – Evidence for Nucleotide Dependent Conformational Changes. Biochemistry 43, 1376-1385.

  • Friedrich, T. & Böttcher, B. (2004) The gross structure of the respiratory complex I: A Lego-System. Biochim. Biophys. Acta 1608, 1-9.

  • Flemming, D., Schlitt, A., Spehr, V., Bischof, T. & Friedrich, T. (2003) Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on NuoB. J. Biol. Chem. 278, 47602-47609.

  • Gong, X., Xie, T., Yu, L., Hesterberg, M., Scheide, D., Friedrich, T. & Yu, C.A. (2003) The Ubiquinone-binding Site in NADH:Ubiquinone Reductase from Escherichia coli, J. Biol. Chem. 278, 25731-25737.

  • Flemming, D., Hellwig, P. & Friedrich, T. (2003) Involvement of tyrosines 114 and 139 of subunit NuoB in the proton pathway around cluster N2 in Escherichia coli NADH:ubiquinone oxidoreductase. J. Biol. Chem. 278, 3055-3062.

  • Scheide, D., Huber, R. & Friedrich, T. (2002) The proton-pumping NADH:ubiquinone oxidoreductase (complex I) from Aquifex aeolicus. FEBS Lett. 512, 80-84.

  • Böttcher, B., Scheide, D., Hesterberg, M., Nagel-Steger, L. & Friedrich, T. (2002) A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I). J. Biol. Chem. 277, 17970-17977.

  • Duarte, M., Populo, H., Videira, A., Friedrich, T. & Schulte, U. (2002) Location and role of iron-sulfur cluster N2 from NADH:quinone oxidoreductase. Biochem. J. 364, 833-839.

  • Arndt, S., Emde, U., Friedrich, T., Grubert, L. & Koert, U. (2001) Quinone-Annonaceous Acetogenins: Synthesis and Complex I Inhibition Studies of a new class of Natural Product Hybride. Chem. Eur. J. 7, 993-1005.

  • Friedrich, T. (2001) Complex I: A chimaera of redox and conformation driven proton-pump? J. Bioenerg. Biomembr. 33, 169-177.

  • Rasmussen, T., Scheide, D., Brors, B., Kintscher, L., Weiss, H. & Friedrich, T. (2001) Characterization of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry 40, 6124-6131.

  • Hellwig, P., Scheide, D., Bungert, S., Mäntele, W. & Friedrich, T. (2000) FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an Aspartate or Glutamate side chain. Biochemistry 39, 10884-10891.

  • Bäurle, S., Peters, U., Friedrich, T. & Koert, U. (2000) Synthesis of (4R,12S,15S,16S,19R, 20R,34S)-Muricatetrocin and (4R,12R,15S,16S,19R,20R,34S)-Muricatetrocin, Two Potent Inhibitors of Mitochondrial Complex I. Eur. J. Org. Chem. 2000, 2207-2217.

  • Friedrich, T. & Scheide, D. (2000) The respiratory complex I of Bacteria, Archaea, and Eucarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479, 1-5.

  • Friedrich, T., Brors, B., Hellwig, P., Kintscher, L., Scheide, D., Schulte, U., Rasmussen, T., Mäntele, W. & Weiss, H. (2000) Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta 1459, 305-310.

  • Barker, H.C., Kinsella, N., Jaspe, A., Friedrich, T. & O’Connor, C.D. (2000) Formate protects stationary phase Escherichia coli and Salmonells cells from killing by a cationic antimicrobial peptide. Mol. Microbiol. 35, 1518-1529.

  • Hoppen, S., Emde, U., Friedrich, T., Grubert, L. & Koert, U. (2000) Natural Product Hybride: Design, Synthesis and Biological Evaluation of Quinone-Annonacae Acetogenins. Angew. Chem. Int. Ed. 39, 2099-2102.

  • Schulte, U., Haupt, V., Abelmann, A., Fecke, W., Brors, B., Rasmussen, T., Friedrich, T. & Weiss, H. (1999) A Reductase/Isomerase Subunit of Mitochondrial NADH:Ubiquinone Oxidoreductase (complex I) Carries an NADPH and is involved in the Biogenesis of the Complex. J. Mol. Biol. 292, 569-580.

  • Bungert, S., Krafft, B., Schlesinger, R. & Friedrich, T. (1999) One-step purification of the NADH dehydrogenase fragment of the Escherichia coli by means of Strep-tag affinity chromatography. FEBS Lett. 460, 207-211.

  • Spehr, V., Schlitt, A., Scheide, D., Guénebaut, V. & Friedrich, T. (1999) Overexpression of the Escherichia coli nuo-Operon and Isolation of the Overproduced NADH:Ubiquinone Oxidoreductase (Complex I). Biochemistry 38, 16261-16267.

  • Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K. & Friedrich, T. (1998) Consistent Structure Between Bacterial and Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I). J. Mol. Biol. 276, 105-112.

  • Braun, M., Bungert, S. & Friedrich, T. (1998) Characterization of the Overproduced NADH Dehydrogenase Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli. Biochemistry 37, 1861-1867.

  • Friedrich, T. (1998) The NADH:Ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta 1364, 134-146.

  • Schröter, T., Hatzfeld, O.M., Gemeinhardt, S., Korn, M., Friedrich, T., Ludwig, B. & Link, T. (1998) Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans. Eur. J. Biochem. 255, 100-106.

  • Friedrich, T. & Weiss, H. (1997) Modular Evolution of the Respiratory NADH:Ubiquinone Oxidoreductase and the Origin of its Modules. J. Theoret. Biol. 187, 529-541.

  • Laval-Favre, K., Letouvet-Pawlak, B., Friedrich, T., Alexandre, J. & Guespin-Michel, J.F. (1997) A gene involved in both protein secretion during growth and starvation-induced development encodes a subunit of the NADH:ubiquinone oxidoreductase in Myxococcus xanthus. Mol. Microbiol. 23, 1043-1052.

  • Friedrich, T. & Weiss, H. (1996) Origin and Evolution of the proton-pumping NADH:Ubiquinone Oxidoreductase (Complex I). In: Origin and Evolution of Biological Energy Conversion, Baltscheffsky, H. ed; pp.205-220, VCH Publishers, New York.

  • Leif, H., Sled, V.D., Ohnishi, T., Weiss, H. & Friedrich, T. (1995) Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230, 538-548.

  • Friedrich, T., Steinmüller, K. & Weiss, H. (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367, 107-111.

  • Friedrich, T., van Heek, P., Leif, H., Ohnishi, T., Forche, E., Kunze, B., Jansen, R., Trowitzsch-Kienast, W., Höfle, G., Reichenbach, H. & Weiss, H. (1994) Two binding sites of inhibitors in NADH:ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase. Eur. J. Biochem. 219, 691-698.

  • Weidner, U., Geier, S., Ptock, A., Friedrich, T., Leif, H. & Weiss, H. (1993) 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 the mitochondrial complex I. J. Mol. Biol. 233, 109-122.

  • Friedrich, T., Weidner, U., Nehls, U., Fecke, W., Schneider, R. & Weiss, H. (1993) Attempts to Define Distinct Parts of NADH:Ubiquinone Oxidoreductase (Complex I). J. Bioenerg. Biomembr. 25, 331-339.

  • Nehls, U., Friedrich, T., Schmiede, A., Ohnishi, T. & Weiss, H. (1992) Characterization of Assembly Intermediates of NADH:Ubiquinone Oxidoreductase (Complex I) Accumulated in Neurospora Mitochondria by Gene Disruption. J. Mol. Biol. 227, 1032-1042.

  • Weiss, H., Friedrich, T., Hofhaus, G. & Preis, D. (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197, 563-576.

  • Weiss, H. & Friedrich, T. (1991) Redox-Linked Proton Translocation by NADH-Ubiquinone Reductase (Complex I). J. Bioenerg. Biomembr. 23, 743-754.

  • Friedrich, T., Strohdeicher, M., Hofhaus, G., Preis, D., Sahm, H. & Weiss, H, (1990) The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase. FEBS Lett. 265, 37-40.

  • Friedrich, T., Hofhaus, G., Ise, W., Nehls, U. Schmitz, B. & Weiss, H. (1989) A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa. Eur. J. Biochem. 180, 173-180.