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ORCID : 0000-0002-0813-7883 ORCID iD

A list of publications including links to all freely available documents can also be found via the University of Freiburg's research information system "FreiDok Plus":

https://freidok.uni-freiburg.de 

2023

 

  • Fix, I., Heidinger, L., Friedrich, T. and Layer, G. (2023) The Radical SAM Heme Synthase AhbD from Methanosarcina barkeri Contains Two Auxiliary [4Fe-4S] Clusters. Biomolecules, 13, 1268.
    doi.org/10.3390/biom13081268
  • Kägi, J., Sloan, W., Schimpf, J., Nasiri, H.R., Lashley, D. and Friedrich, T. (2023) Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidases. Sci. Rep., 13, 12226. 10.1038/s41598-023-39430-w.
  • Strotmann, L., Harter, C., Gerasimova, T., Ritter, K., Jessen, H.J., Wohlwend, D. and Friedrich, T. (2023) H2O2 selectively damages the binuclear iron-sulfur cluster N1b of respiratory complex I. Sci. Rep., 13, 7652. 10.1038/s41598-023-34821-5.
  • Makarchuk, I., Gerasimova, T., Kägi, J., Wohlwend, D., Melin, F., Friedrich, T. and Hellwig, P. (2023) Mutating the environment of heme b595 of E. coli cytochrome bd-I oxidase shifts its redox potential by 200 mV without inactivating the enzyme. Bioelectrochemistry, 151, 108379. 10.1016/j.bioelechem.2023.108379.

 

2022

 
  • Makarchuk, I., Kägi, J., Gerasimova, T., Wohlwend, D., Friedrich, T., Melin, F. and Hellwig, P. (2022) pH-dependent kinetics of NO release from E. coli bd-I and bd-II oxidase reveals involvement of Asp/Glu58B. Biochim. Biophys. Acta, 1863, 148952. https://doi: 10.1016/j.bbabio.2022.148952
  • Kägi, J., Makarchuk, I., Wohlwend, D., Melin, F., Friedrich, T. and Hellwig, P. (2022) E. coli cytochrome bd-I requires Asp58 in the CydB subunit for catalytic activity. FEBS Lett., 596, 2418-2424. https://doi: 10.1002/1873-3468.14482
  • Oppermann, S., Seng, K., Shweich, L. and Friedrich, T. (2022) The gene order in the nuo-operon is not essential for the assembly of E. coli complex I. Biochim. Biophys. Acta, 1863, 148592. https://doi.org/10.1016/j.bbabio.2022.148592
  • Gagsteiger, J., Jahn, S., Heidinger, L., Gericke, L., Andexer, J.N., Friedrich, T., Loenarz, C. and Layer, G. (2022) A Cobalamin-Dependent Radical SAM Enzyme Calalyzes the Unique Cα-Methylation of Glutamine in Methyl-Coenzyme M Reductase. Angew. Chem. Int. Ed., e202204198. https://doi.org/10.1002/anie.202204198
  • Hoeser, F., Tausend, H., Götz, S., Wohlwend, D., Einsle, O., Günther, S. and Friedrich, T. (2022) Respiratory complex I with charge symmetry in the membrane arm pumps protons. Proc. Natl. Acad. Sci., 119, e2123090119. https://doi.org/10.1073/pnas.2123090119
  • Friedrich, T., Wohlwend, D. and Borisov, V.B. (2022) Recent Advances in Structural Studies of Cytochrome bd and Its Potential Application as a Drug Target. Int. J. Mol. Sci. 23, 3166. https://doi.org/10.3390/ijms23063166
  • Hoeser, F., Weiß, M. and Friedrich, T. (2022) The clinically relevant triple mutation in the mtND1 gene inactivates Escherichia coli complex I. FEBS Lett., 596, 1124-1132. https://doi.org/10.1002/1873-3468.14325
  • Van den Bergh, B., Schramke, H., Michiels, J., Kimkes, T., Radzikowski, J., Schimpf, J., Vedelaar, S., Burschel, S., Dewachter, L., Loncar, N., Schmidt, A., Meijer, T., Fauvart, M., Friedrich, T., Michiels, J. and Heinemann, M. (2022) Mutations in respiratory complex I promote antibiotic persistence through alterations in intracellular acidity and protein synthesis. Nat. Commun., 13:54. https://doi.org/10.1038/s41467-022-28141-x
  • Schimpf, J., Oppermann, S., Gerasimova, T., Santos Seica, A.F., Hellwig, P., Grishkovskaya, I., Wohlwend, D., Haselbach, D. and Friedrich, T. (2022) Structure of the peripheral arm of a minimalistic respiratory complex I. Structure, 30, 80-94.e4. https://doi.org/10.1016/j.str.2021.09.005

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2021

 

  • Hagel, C., Blaum, B., Friedrich, T. and Heider, J. (2021) Characterisation of the redox centers of ethylbenzene dehydrogenase. J. Biol. Inorg. Chem., https://doi.org/10.1007/s00775-021-01917-0
  • Grauel, A., Kägi, J., Rasmussen, T., Makarchuk, I., Oppermann, S., Moumbock, A.F.A., Wohlwend, D., Müller, R., Melin, F., Günther, S., Hellwig, P., Böttcher, B. and Friedrich, T. (2021) Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D. Nature Commun., 12:6498. https://doi.org/10.1038/s41467-021-26835-2
  • Vranas, M., Wohlwend, D., Qiu, D., Gerhardt, S., Trncik, C., Pervaiz, M., Ritter, K., Steimle, S., Randazzo, A., Einsle, O., Günther, S., Jessen, H.J., Kotlyar, A. and Friedrich, T. (2021) Structural Basis for Inhibition of ROS-Producing Respiratory Complex I by NADH-OH. Angew. Chem. Int. Ed., https://doi.org/10.1002/anie.202112165
  • Schimpf, J., Oppermann, S., Gerasimova, T., Santos Seica, A.F., Hellwig, P., Grishkovskaya, I., Wohlwend, D., Haselbach, D. and Friedrich, T. (2021) Structure of the peripheral arm of a minimalistic respiratory complex I. Structure, https://doi.org/10.1016/j.str.2021.09.005
  • Nuber, F., Schimpf, J., di Rago, J.-P., Tribouillard-Tanvier, D., Procaccio, V., Martin-Negrier, M.-L., Trimouille, A., Biner, O., von Ballmoos, C. and Friedrich, T. (2021) Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli respiratory complex I. Sci. Rep., 11, 12641. DOI: 10.1038/s41598-021-91631-3.
  • Makarchuk, I., Nikolaev, A., Thesseling, A., Dejon, L., Lamberty, D., Stief, L., Speicher, A. Friedrich, T., Hellwig, P., Nasiri, H.R. and Melin, F. (2021) Identification and optimization of quinolone-based inhibitors against cytochrome bd oxidase using an electrochemical assay. Electrochim. Acta 381, 138293. DOI: 10.1016/j.electacta.2021.138293
  • Nuber, F., Merono, L., Oppermann, S., Schimpf, J., Wohlwend, D. and Friedrich, T. (2021) A quinol anion as catalytic intermediate coupling proton translocation with electron transfer in E. coli respiratory complex I. Front. Chem., 9, 672969. DOI: 10.3389/fchem.2021.672969
  • Nikolaev, A., Safarian, S., Thesseling, A., Wohlwend, D., Friedrich, T., Michel, H., Kusomoto, T., Sakamoto, J., Melin, F. and Hellwig, P. (2021) Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms. Biochim. Biophys. Acta, 1862, 148436. DOI: 10.1016/j.bbabio.2021.148436
  • Olerinyova, A., Sonn-Segev, A., Gault, J., Eichmann, C., Schimpf, J., Kopf, A.H., Rudden, L.S.P., Ashkinadze, D., Bomba, R., Frey, L., Greenwald, J., Degiacomi, M.T., Steinhilper, R., Killian, A., Friedrich, T., Riek, R., Struwe, W.B. and Kukura, P. (2021) Mass Photometry of Membrane Proteins. Chem 7, 1-13. DOI: 10.1016/j.chempr.2020.11.011

2020 - 2016

 

  • Oppermann, S., Höfflin, S. and Friedrich, T. (2020) ErpA is important but not essential for the Fe/S cluster biogenesis of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta, 1861:148286. DOI: j.bbabio.2020.148286.
  • Kuhns, M., Schuchmann, V., Schmidt, S., Friedrich, T., Wiechmann, A. and Müller, V. (2020) The Rnf complex from the acetogenic bacterium Acetobacterium woodii: Purification and characterization of RnfC and RnfB. Biochim. Biophys. Acta, 1861:148263. DOI: j.bbabio.2020.148263.
  • Nikolaev, A., Makarchuk, I., Thesseling, A., Hoeser, J., Friedrich, T., Melin, F. and Hellwig, P. (2020) Stabilization of the highly hydrophobic membrane protein cytochrome bd oxidase on metallic surfaces for direct electrochemical studies. Molecules, 25, 3240. DOI:10.3390/molecules25143240.
  • Mühlbauer, M., Saura, P., Nuber, F., Di Luca, A., Friedrich, T. and Kaila, V. (2020) Water-Gated Proton Transfer Dynamics in Respiratory Complex I. J. Am. Chem. Soc.,142,13718-13728. DOI: 10.1021/jacs.0c02789.
  • Bittner, T., Wittwer, C., Hauke, S., Wohlwend, D., Mundinger, S., Dutta, A., Bezold, D., Dürr, T., Friedrich, T., Schultz, C. and Jessen, H. (2020) Photolysis of caged inositol-pyrophosphate InsP8 directly modulates intracellular Ca2+oscillations and controls C2AB domain localization. J. Am. Chem. Soc.142, 10606-10611. DOI: 10.1021/jacs.0c01697.
  • Sonn-Segev, A., Belacic, K., Bodrug, T., Young, G., VanderLinden, R.T., Schulman, B.A., Schimpf, J., Friedrich, T., Dip, P.V., Schwartz, T.U., Bauer, B., Peters, J.-M., Struwe, W.B., Benesch, J.L.P., Brown, N.G., Haselbach, D. and Kukura, P. (2020) Quantifying the heterogeneity of macromolecular machines by mass photometry. Nature Commun. 11:1772. DOI: 10.1038/s41467-020-15642-w.
  • Theßeling, A., Burschel, S., Wohlwend, D. and Friedrich, T. (2020) The long Q-loop of Escherichia coli cytochrome bd oxidase is required for assembly and structural integrity. FEBS Lett. 594, 1577-1585. DOI: 10.1002/1873-3468.13749.
  • Skorupa, P., Lindenstrauß, U., Burschel, S., Blumenscheit, C., Friedrich, T. and Pinske, C. (2020) The N-terminal Domains of the Paralogous HycE and NuoCD Govern Assembly of the Respective Formate Hydrogenlyase and NADH Dehydrogenase Complexes. FEBS Open Bio 10, 371-385. DOI: 10.1002/2211-5463.12787.
  • Santos Seica, A.F., Schimpf, J., Friedrich, T. and Hellwig, P. (2019) Visualizing the movement of the amphipathic helix in the respiratory complex I using a nitrile infrared probe and SEIRAS. FEBS Lett. 594, 491-496. DOI: 10.1002/1873-3468.13620.
  • Theßeling, A., Rasmussen, T., Burschel, S., Wohlwend, D., Kägi, J., Müller, R., Böttcher, B., and Friedrich, T. (2019) Homologous bd oxidases share the same architecture but differ in mechanism. Nature Comm. 10:5138. DOI: 10.1038/s41467-019-13122-4.
  • Marckmann, D., Trasnea, P.-I., Schimpf, J., Winterstein, C., Andrei, A., Schmollinger, S., Blaby-Haas, C.E., Friedrich, T., Daldal, F. and Koch, H.G. (2019) The cbb3-type cytochrome oxidase assembly factor CcoG is a widely distributed novel cupric reductase. Proc. Natl. Acad. Sci. USA 116, 21166-21175. DOI: 10.1073/pnas.1913803116.
  • Schulte, M., Frick, K., Gnandt, E., Jurkovic, S., Burschel, S., Labatzke, R., Aierstock, K., Fiegen, D., Wohlwend, D., Gerhardt, S., Einsle, O. and Friedrich, T. (2019) A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I. Nature Comm. 10: 2551. DOI: 10.1038/s41467-019-10429.
  • Wissig, J., Grischin, J., Bassler, J., Schubert, C., Friedrich, T., Schultz, J.E. and Unden, G. (2019) CyaC, a redox-regulated adenylate cyclase of Sinorhizobium meliloti with a quinone responsive diheme-B membrane anchor domain. Mol. Microbiol. 112, 16-28. DOI:10.1111/mmi.14251.
  • Burschel, S., Kreuzer Decovic, D., Nuber, F., Stiller, M., Hofmann, M., Zupok, A., Siemiatkowska, B., Gorka, M., Leimkühler, S. and Friedrich, T. (2019) Iron-Sulfur Cluster Carrier Proteins Involved in the Assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Mol. Microbiol. 111, 31-45. DOI: 10.1111/mmi.14137.
  • Na, S., Jurkovic, S., Friedrich, T. and Koslowski, T. (2018) Charge transfer through a fragment of the respiratory complex I and its regulation: an atomistic simulation approach. Phys. Chem. Chem. Phys., 20, 20023-20032; DOI: 10.1039/c8cp02420k.
  • Hoeser, J., Gnandt, E. and Friedrich, T. (2018) Low cost, multi-wavelength microcontroller based heating device for differential scanning fluorimetry. Sci. Rep., 8:1457. DOI: 10.1038/s41598-018-19702-6.
  • Gnandt, E., Schimpf, J., Harter, C., Hoeser, J. and Friedrich, T. (2017) Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation. Sci. Rep., 7:8754. DOI:10.1038/s41598-017-09345-4. 
  • Dörner, K., Vranas, M., Schimpf, J., Straub, I.R., Hoeser, J. and Friedrich T. (2017) Significance of the [2Fe-2S] Cluster N1a for Electron Transfer and Assembly of Escherichia coli Respiratory Complex I. Biochemistry, 56, 2770-2778. DOI: 10.1021/acs.biochem.6b01058
  • Greule, A., Marolt, M., Deubel, D., Peintner, I., Zhang, S., Jessen-Trefzer, C., De Ford, C., Burschel, S., Li, S.-M., Friedrich, T., Merfort, I., Lüdeke, S., Bisel, P., Müller, M., Paululat, T. and Bechthold, A. (2017) Wide Distribution of Foxicin Biosynthetic Gene Clusters in Streptomyces Strains – An Unusual Secondary Metabolite with Various Properties. Front. Microbiol. 8:221. DOI: 10.3389/fmicb.2017.00221
  • Arias-Cartin, R., Ceccaldi, P., Schoepp-Cothenet, B., Frick, K., Blanc, J.-M., Guigliarelli, B., Walburger, A., Grimaldi, S., Friedrich, T., Receveur-Brechot, V., and Magalon, A. (2016) Redox cofactor insertion in prokaryotic molybdoenzymes occurs via a conserved structural mechanism. SciRep. 6:37743. DOI: 10.1038/srep37743.
  • Fournier, E., Nikolaev, A., Nasiri, H., Hoeser, J., Friedrich, T., Hellwig, P. and Melin, F. (2016) Creation of a gold nanoparticles-based electrochemical biosensor for identification of inhibitors of bacterial cytochrome bd oxidases. Bioelectrochemistry 111, 109-114.
  • Al-Attar, S., Yu, Y., Pinske, M., Hoeser, J., Friedrich, T., Bald, D. and de Vries, S. (2016) Cytochrome bd Displays Significant Quinol Peroxidase Activity. Sci. Rep. 6:27631.
  • Gnandt, E., Dörner, K., Strampraad, M.F.J., de Vries, S. and Friedrich, T. (2016) The multitude of iron-sulfur clusters in respiratory complex I. Biochim. Biophys Acta, 1857, 1068-1072.
  • De Ford, C., Heidersdorf, B., Murillo,R., Friedrich, T., Borner, C., Haun, F. and Merfort, I. (2016) The clerodane diterpene casearin J induces apoptosis of T-ALL cells through SERCA inhibition, oxidative stress and interference with Notch1 signaling. Cell Death Dis., 7:e2070.
  • Hellwig, P., Kriegel, S. and Friedrich, T. (2016) Infrared spectroscopic studies on reaction induced conformational changes in the NADH ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta, 1857, 922-927.
  • Friedrich, T., Kreuzer-Dekovic, D. and Burschel, S. (2016) Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I). Biochim. Biophys. Acta, 1857, 214-223.

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2015 - 2011
  • Kriegel, S., Srour, B., Steimle, S., Friedrich, T. and Hellwig, P. (2015) Involvement of acidic amino acid residues in Zn2+ binding to respiratory complex I. ChemBioChem, 16, 2080-2085.
  • Steimle, S., Schnick, C., Burger, E-M, Nuber, F., Krämer, D., Dawitz, H., Brander, S., Matlosz, B., Schäfer, J., Maurer, K., Glessner, U. and Friedrich, T. (2015) Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I. Mol. Microbiol., 98, 151-161.
  • Frick, K., Schulte, M. and Friedrich, T. (2015) Reactive Oxygen Species Production by Escherichia coli Respiratory Complex I. Biochemistry, 54, 2799-2801. (“Highlight Beitrag” der Biochemistry Ausgabe)
  • De Vries, S., Dörner, K., Strampraad, M.F.J. and Friedrich, T. (2015) Electron tunneling Rates in Complex I Are Tuned for Efficient Energy Conversion. Angew. Chem. Int. Ed., 54, 2844-2848 („VIP-Manuskript“).
  • De Vries, S., Dörner, K., Strampraad, M.F.J. and Friedrich, T. (2015) Die Elektronentunnelraten im Atmungskettenkomplex I sind auf eine effiziente Energiewandlung abgestimmt. Angew. Chem., 127, 2886-2890.
  • Kriegel, S., Uchida, T., Osawa, M., Friedrich, T. and Hellwig, P. (2014) A biomimetic environment to study E. coli Complex I through Surface Enhanced IR Absorption Spectroscopy (SEIRAS). Biochemistry, 53, 6340-6347.
  • Schulte, M., Mattay, D., Kriegel, S., Hellwig, P. and Friedrich, T. (2014) Inhibition of Escherichia coli Respiratory Complex I by Zn2+. Biochemistry, 53, 6332-633986. 
  • Friedrich, T. (2014) On the mechanism of respiratory complex I. J. Bioenerg. Biomembr. 46, 255-268.
  • Hoeser, J., Hong, S., Gehmann, G., Gennis, R.B. and Friedrich, T. (2014) Subunit CydX of Escherichia colicytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site. FEBS Lett., 588, 1537-1541.
  • Erhardt, H., Dempwolff, F., Pfreundschuh, M., Riehle, M., Schäfer, C., Pohl, T., Graumann, P. and Friedrich, T. (2014) Organization of the Escherichia coli aerobic enzyme complexes of oxidative phosphorylation in dynamic domains within the cytoplasmic membrane. MicrobiologyOpen, 33, 316-326.
  • Llorente-Garcia, I., Lenn, T., Erhardt, H., Harriman, O.L., Liud, L., Robson, A., Chiua, S-W., Matthews, S., Willis, N.J., Brayd, C.D., Liphardt, J., Friedrich, T., Mullineaux, C.W. and Leake, M.C. (2014) Dynamic visualization of oxidative phosphorylation machinery in vivo shows delocalization of electron transport and proton-motive force. Biochim. Biophys. Acta, 1837, 811-824.
  • Kloss, F., Pidot, S., Goerls, H., Friedrich, T. and Hertweck, C. (2013) Formation of a Dinuclear Copper(I) Complex from the Clostridium-Derived Antibiotic Closthioamide. Angew. Chem. Int. Ed., 52, 10745-10748.
  • Hielscher, R., Yegres, M., Voicescu, M., Gnandt, E., Friedrich, T. and Hellwig, P. (2013) Characterization of two quinone radicals in the NADH:ubiquinone oxidoreductase from Escherichia coli by a combined fluorescence spectroscopic and electrochemical approach. Biochemistry, 52, 8993-9000.
  • Birrell, J.A., Morina, K., Bridges, H.R., Friedrich, T. and Hirst, J. (2013) Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential. Biochem. J., 456, 139-146
  • Teufel, R., Friedrich, T. and Fuchs, G. (2012) An oxygenase that forms and deoxygenates toxic epoxide. 
    Nature, 483, 359-362.
  • Steimle, S., Willistein, M., Hegger, P., Janoschke, M., Erhardt, H. and Friedrich, T. (2012) Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I. FEBS Lett., 586, 699-704.
  • Erhardt, H., Steimle, S., Muders, V., Pohl, T., Walter, J. and Friedrich, T. (2012) Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochim. Biophys. Acta, 1817, 863-871.
  • Hilberg, M., Pierik, A.J., Bill, E., Friedrich, T., Lippert, M.L. and Heider, J. (2012) Identification of FeS clusters in the glycyl-radical enzyme benzylsuccinate synthase via EPR and Mössbauer spectroscopy. J. Biol. Inorg. Chem. 17, 49-56.
  • Morina, K., Schulte, M., Hubrich, F., Dörner, K., Steimle, S., Stolpe, S. and Friedrich, T. (2011) Engineering the respiratory complex I to an energy-converting NADPH:ubiquinone oxidoreductase. J. Biol. Chem. 286, 34267-34634.
  • Steimle, S., Bajzath, C., Dörner, K., Schulte, M., Bothe, V. and Friedrich, T. (2011) Role of Subunit NuoL for Proton Translocation by Respiratory Complex I. Biochemistry 50, 3386-3393.
  • Krätzer, C., Welte, C., Dörner, K., Friedrich, T. and Deppenmeier, U. (2011) Characterization of methanoferrodoxin: a novel superoxide reductase. FEBS J., 278, 442-451.
  • Hielscher, R., Friedrich, T. and Hellwig, P. (2011) Far and mid infrared spectroscopic analysis on the substrate induced structural dynamics of the respiratory complex I. ChemPhysChem, 12, 217-224. 
  
2010 - 2000
  • Pohl, T., Spatzal, T., Aksoyoglu, M., Schleicher, E., Rostas, A.M., Lay, H., Glessner, U., Boudon, C., Hellwig, P., Weber, S. and Friedrich, T. (2010) Spin-labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta, 1797, 1894-1900.
  • Friedrich, T. and 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.
  • Dorn, K.V., Willmund, F., Schwarz, C., Henselmann, C., Pohl, T., Heß, B., Usadel, B., Friedrich, T., Nickelsen, J. and Schroda, M. (2010) Chloroplast DnaJ homologs 3 and 4 (CDJ3/4) from Chlamydomonas reinhardtii contain redox-active iron-sulfur clusters and interact with stromal HSP70B. Biochem. J., 427, 205-215.
  • Graff, A., Fraysse-Ailhas, C., Palivan, C.G., Grzelakowski, M., Friedrich, T., Vebert, C., Gescheidt, G. and Meier, W. (2010) Amphiphilic Copolymer membranes promote NADH:Ubiquinone Oxidoreductase activity: Towards an Electron-Transfer Nanodevice. Macromol. Chem. Phys., 211, 229-238.
  • Kung, J., Löffler, C., Dörner, K., Heintz, D., Gallien, S., Van Dorsselaer, A, Friedrich, T. and Boll, M. (2009) Identification and characterization of the tungsten-containing class of benzoyl-coenzyme A reductases. Proc. Natl. Acad. Sci USA, 106, 17687-17692.
  • Wittekind, C., Schwarz, M., Friedrich, T. and Koslowski, T. (2009) Aromatic Amino 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.
  • Schoepp-Cothenet, B., Lieutaud, C., Baymann, F., Vermeglio, A., Friedrich, T., Kramer, D.M. and Nitschke, W. (2009) Menaquinone as pool quinone in a purple bacterium. Proc. Natl. Acad. Sci USA 106, 8549-8554.
  • Kohlstädt, M., Dörner, K., Labatzke, R., Koç, C., Hielscher, R., Schiltz, E., Einsle, O., Hellwig, P. and 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. and 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. and Friedrich, T. (2008) Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta 1777, 735-739.
  • Johannes, J., Unciuleac, M-C., Friedrich, T., Warkentin, E., Ermler, U. and 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. and 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. and 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. and 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. and 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. and 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. and 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. and Bechthold, A. (2006) The Active Conformation of Avilamycin A is Confered by AviX12, a Radical AdoMet Enzyme. J. Biol. Chem. 281, 14756-14763.
  • Hielscher, R., Wenz, T., Stolpe, S., Hunte, C., Friedrich, T. and 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. and 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, 208-222.
  • Utz, N., Engel, L., Friedrich, T. and Koslowski, T. (2005) A variational approach to protein charge transfer. Z. Phys. Chem. 219, 1391-1410.
  • 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. and Hackstein, J.H.P. (2005) An anaerobic mitochondrion that produces hydrogen. Nature 434, 74-79.
  • Friedrich, T., Stolpe, S., Schneider, D., Barquera, B. and Hellwig, P. (2005) Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochem. Soc. Trans. 33, 836-839.
  • Uhlmann, M. and Friedrich, T. (2005) 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. and 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., and Friedrich, T. (2004) FTIR spectroscopic study on the conformational reorganization in E. coli complex I due to redox-driven proton translocation. Biopolymers 74, 69-72.
  • Stolpe, S. and Friedrich, T. (2004) The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton-pump but may be capable of secondary sodium antiport. J. Biol. Chem. 279, 18377-18383.
  • Möbitz, H., Friedrich, T. and Boll, M. (2004) Substrate Binding and Reduction of Benzoyl-CoA Reductase: Evidence for Nucleotide Dependent Conformational Changes. Biochemistry 43, 1376-1385.
  • Friedrich, T. and 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. and Friedrich, T. (2003) Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB. J. Biol. Chem. 278, 47602-47609.
  • Gong, X., Xie, T., Yu, L., Hesterberg, M., Scheide, D., Friedrich, T. and Yu, C.A. (2003) The Ubiquinone-binding Site in NADH:Ubiquinone Oxidoreductase from Escherichia coli. J. Biol. Chem. 278, 25731-25737.
  • Flemming, D., Hellwig, P. and 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.
  • Duarte, M., Populo, H., Videira, A., Friedrich, T. and Schulte, U. (2002) Disruption of iron-sulphur cluster N2 from NADH: ubiquinone oxidoreductase by site-directed mutagenesis. Biochem. J. 364, 833-839.
  • Böttcher, B., Scheide, D., Hesterberg, M., Nagel-Steger, L. and Friedrich, T. (2002) A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I). J. Biol. Chem. 277, 17970-17977.
  • Scheide, D., Huber, R. and Friedrich, T. (2002) The proton-pumping NADH:ubiquinone oxidoreductase (complex I) from Aquifex aeolicus. FEBS Lett. 512, 80-84.
  • Rasmussen, T., Scheide, D., Brors, B., Kintscher, L., Weiss, H. and Friedrich, T. (2001) Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry 40, 6124-6131.
  • Friedrich, T. (2001) Complex I: A chimaera of a redox and conformation driven proton-pump? J. Bioenerg. Biomembr. 33, 169-177.
  • Arndt, S., Emde, U., Friedrich, T., Grubert, L. and 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.
  • Hellwig, P., Scheide, D., Bungert, S., Mäntele, W. and 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.
  • Friedrich, T., Brors, B., Hellwig, P., Kintscher, L., Scheide, D., Schulte, U., Rasmussen, T., Mäntele, W. and Weiss, H. (2000) Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta 1459, 305-310.
  • Friedrich, T. and 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.
  • Bäurle, S., Peters, U., Friedrich, T. and 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.
  • Hoppen, S., Emde, U., Friedrich, T., Grubert, L. and Koert, U. (2000) Natural Product Hybride: Design, Synthesis and Biological Evaluation of Quinone-Annonacae Acetogenins. Angew. Chem. Int. Ed. 39, 2099-2102.
  • Barker, H.C., Kinsella, N., Jaspe, A., Friedrich, T. and 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.
Publications before 2000
  • Spehr, V., Schlitt, A., Scheide, D., Guénebaut, V. and Friedrich, T. (1999) Overexpression of the Escherichia coli nuo-Operon and Isolation of the Overproduced NADH:Ubiquinone Oxidoreductase (Complex I). Biochemistry 38, 16261-16267.
  • Bungert, S., Krafft, B., Schlesinger, R. and 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.
  • Schulte, U., Haupt, V., Abelmann, A., Fecke, W., Brors, B., Rasmussen, T., Friedrich, T. and 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.
  • Schulte, U., Abelmann, A., Amling, N., Brors, B., Friedrich, T., Kintscher, L., Rasmussen, T. and Weiss, H. (1998) Analysis of the redox groups of mitochondrial NADH:ubiquinone oxidoreductase (complex I ) by UV/VIS-spectroscopy. BioFactors 8, 177-186.
  • Schröter, T., Hatzfeld, O.M., Gemeinhardt, S., Korn, M., Friedrich, T., Ludwig, B. and 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., Abelmann, A., Brors, B., Guénebaut, V., Kintscher, L., Leonard, K., Rasmussen, T., Scheide, D., Schlitt, A., Schulte, U. and Weiss, H. (1998) Redox components and structure of the respiratory NADH:Ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta 1365, 215-219.
  • Friedrich, T. (1998) The NADH:Ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta 1364, 134-146.
  • Braun, M., Bungert, S. and Friedrich, T. (1998) Characterization of the Overproduced NADH Dehydrogenase Fragment of the NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli. Biochemistry 37, 1861-1867.
  • Guénebaut, V., Schlitt, A., Weiss, H., Leonard, K. and Friedrich, T. (1998) Consistent Structure Between Bacterial and Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I). J. Mol. Biol. 276, 105-112.
  • Laval-Favre, K., Letouvet-Pawlak, B., Friedrich, T., Alexandre, J. and 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. and Weiss, H. (1997) Modular Evolution of the Respiratory NADH:Ubiquinone Oxidoreductase and the Origin of its Modules. J. Theoret. Biol. 187, 529-541.
  • Dronia, H., Gross, U., Haegele, G., Friedrich, T. and Weiss, H. (1996) Structure-activity analysis of fluorinated 1-N-arylamino-1-arylmethane-phosphonic acids esters as inhibitors of the NADH:ubiquinone oxidoreductase (complex I). J. Comput. Aid. Mol. Des. 10, 100-106.
  • Friedrich, T., Steinmüller, K. and Weiss, H. (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367, 107-111.
  • Leif, H., Sled, V.D., Ohnishi, T., Weiss, H. and Friedrich, T. (1995) Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230, 538-548.
  • Friedrich, T., Ohnishi, T., Forche, E., Kunze, B., Jansen, R., Trowitzsch, W., Höfle, G. Reichenbach, H. and Weiss, H. (1994) Two binding sites for naturally occurring inhibitors in mitochondrial and bacterial NADH:ubiquinone oxidoreductase (Complex I). Biochem. Soc. Trans. 22, 226-230.
  • Friedrich, T., van Heek, P., Leif, H., Ohnishi, T., Forche, E., Kunze, B., Jansen, R., Trowitzsch-Kienast, W., Höfle, G., Reichenbach, H. and 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.
  • Leif, H., Weidner, U., Berger, A., Spehr, V., Braun, M., van Heek, P., Friedrich, T., Ohnishi, T. and Weiss, H. (1993) Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I. Biochem. Soc. Trans. 21, 998-1001.
  • Friedrich, T., Weidner, U., Nehls, U., Fecke, W., Schneider, R. and Weiss, H. (1993) Attempts to Define Distinct Parts of NADH:Ubiquinone Oxidoreductase (Complex I). J. Bioenerg. Biomembr. 25, 331-339.
  • Sled', V.D., Friedrich, T., Leif, H., Weiss, H., Meinhardt, S.W., Fukumori, Y., Calhoun, M., Gennis, R.B. and Ohnishi, T. (1993) Bacterial NADH-Quinone Oxidoreductases: Iron-Sulfur Clusters and Related Problems. J. Bioenerg. Biomembr. 25, 347-356.
  • Weidner, U., Geier, S., Ptock, A., Friedrich, T., Leif, H. and 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.
  • Weidner, U., Nehls, U., Schneider, R., Fecke, W., Leif, H., Schmiede, A., Friedrich, T., Zensen, R., Schulte, U., Ohnishi, T. and Weiss, H. (1992) Molecular genetic studies of complex I in Neurospora crassa, Aspergillus niger and Escherichia coli. Biochim. Biophys. Acta 1101, 177-180.
  • Nehls, U., Friedrich, T., Schmiede, A., Ohnishi, T. and 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.
  • Schmidt, M., Friedrich, T., Wallrath, J., Ohnishi, T. and Weiss, H. (1992) Accumulation of the preassembled membrane arm of NADH:ubiquinone oxidoreductase in mitochondria of manganese-limited grown Neurospora crassa. FEBS Lett. 313, 8-11.
  • Weiss, H. and Friedrich, T. (1991) Redox-Linked Proton Translocation by NADH-Ubiquinone Reductase (Complex I). J. Bioenerg. Biomembr. 23, 743-754.
  • Weiss, H., Friedrich, T., Hofhaus, G. and Preis, D. (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197, 563-576.
  • Friedrich, T., Strohdeicher, M., Hofhaus, G., Preis, D., Sahm, H. and 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. and 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.
 
Book Chapters
  • Friedrich, T., Hellwig, P. and Einsle, O. (2012) On the mechanism of the respiratory complex I. In: A structural perspective on complex I. L.A. Sazanov, ed.; pp. 23-61, Springer, Berlin.
  • Friedrich, T., Pohl, T. and Hellwig, P. (2007) The bacterial NADH:ubiquinone oxidoreductase: Molecular biology, Structure, Spectroscopy and Mechanism. In: Complex I and alternative Dehydrogenases, M.I. Gonzalez Siso, ed.; pp. 1-31, Transworld Research Network, Kerala, India.
  • Friedrich, T. and T. Pohl. (13 August 2007, posting date) Chapter 3.2.4, NADH as Donor. In A. Böck, R. Curtiss III, J. B. Kaper, F. C. Neidhardt, T. Nyström, J. M. Slauch, and C. L. Squires (ed.), EcoSal—Escherichia coli and Salmonella: cellular and molecular biology. http://www.ecosal.org. ASM Press, Washington, D.C.
  • Friedrich, T. and 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.
  • Friedrich, T., Hofhaus, G., Tuschen, G. and Weiss, H. (1991) Two related forms of the respiratory chain NADH dehydrogenase (Complex I) in Neurospora mitochondria. In: Flavins and Flavoproteins 1990, Curti, B., Ronchi, S. and Zanetti, G.; eds; pp.735-738, Walter de Gruyter, Berlin/New York
  • Tuschen, G., Nehls, U., Sackmann, U., Schmidt, M., Friedrich, T., Wang, D.C., Ohnishi, T. and Weiss, H. (1990) Assembly of NADH:ubiquinone reductase in Neurospora mitochondria. In: Structure, function and biogenesis of energy transfer systems, Quagliariello, E., Papa, S., Palmieri, F. and Saccone, C., eds; pp. 47-52, Elsevier Science Publishers B.V.

 
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