Publications of the Department of Molecular Membrane Biology

Elamri, I.; Radloff, M.; Hohmann, K. F.; Nimbarte, V. D.; Nasiri, H. R.; Bolte, M.; Safarian, S.; Michel, H.; Schwalbe, H.: Synthesis and Biological Screening of new Lawson Derivatives as selective substrate‐based Inhibitors of Cytochrome bo₃ Ubiquinol Oxidase from Escherichia coli. ChemMedChem 15 (14), pp. 1262 - 1271 (2020)

Zeng, H.; Zhu, G.; Zhang, S.; Li, X.; Martin, J.; Morgner, N.; Sun, F.; Peng, G.; Xie, H.; Michel, H.: Isolated Heme A Synthase from Aquifex aeolicus Is a Trimer. mBio 11 (3), e02615-19 (2020)

Neuhaus, A.; Selvaraj, M.; Salzer, R.; Langer, J. D.; Kruse, K.; Kirchner, L.; Sanders, K.; Daum, B.; Averhoff, B.; Gold, V.: Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nature Communications 11, 2231 (2020)

Dörrbaum, A. R.; Alvarez-Castelao, B.; Nassim-Assir, B.; Langer, J. D.; Schuman, E. M.: Proteome dynamics during homeostatic scaling in cultured neurons. eLife 9, e52939 (2020)

Vitt, S.; Prinz, S.; Hellwig, N.; Morgner, N.; Ermler, U.; Buckel, W.: Molecular and Low-Resolution Structural Characterization of the Na+-Translocating Glutaconyl-CoA Decarboxylase From Clostridium symbiosum. Frontiers in Microbiology 11, 480 (2020)

Huang, G.; Wagner, T.; Demmer, U.; Warkentin, E.; Ermler, U.; Shima, S.: The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase. Journal of Molecular Biology (London) 432 (7), pp. 2042 - 2054 (2020)

Huang, G.; Wagner, T.; Ermler, U.; Shima, S.: Methanogenesis involves direct hydride transfer from H₂ to an organic substrate. Nature Reviews Chemistry 4 (2), pp. 213 - 221 (2020)

Biever, A.; Glock, C.; Tushev, G.; Ciirdaeva, E.; Dalmay, T.; Langer, J. D.; Schuman, E. M.: Monosomes actively translate synaptic mRNAs in neuronal processes. Science 367 (6477), eaay4991, p. 526 (2020)

Zhu, G.; Zeng, H.; Zang, S.; Juli, J.; Pang, X.; Hoffman, J.; Zhang, Y.; Morgner, N.; Zhu, Y.; Peng, G. et al.; Michel, H.; Sun, F.: A 3.3 Å‐Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of its Thermal Stability. Angewandte Chemie, International Edition in English 59 (1), pp. 343 - 351 (2020)

Brünle, S.; Eisinger, M. L.; Poppe, J.; Mills, D. J.; Langer, J. D.; Vonck, J.; Ermler, U.: Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism. Proceedings of the National Academy of Sciences of the United States of America 52 (116), pp. 26497 - 26504 (2019)

Lencina, A. M.; Koepke, J.; Preu, J.; Münke, C.; Gennis, R. B.; Michel, H.; Schurig-Briccio, L. A.: Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus. Biochimica et Biophysica Acta, Bioenergetics 1860 (11), e148080 (2019)

Safarian, S.; Hahn, A.; Mills, D.; Radloff, M.; Eisinger, M. L.; Nikolaev, A.; Meier-Credo, J.; Melin, F.; Miyoshi, H.; Gennis, R.B. et al.; Sakamoto, J.; Langer, J. D.; Hellwig, P.; Kühlbrandt, W.; Michel, H.: Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science 366 (6461), pp. 100 - 104 (2019)

Kourpa, K.; Manarolaki, E.; Lyratzakis, A.; Strataki, V.; Rupprecht, F. A.; Langer, J. D.; Tsiotis, G.: Proteome Analysis of Enriched Heterocysts from Two Hydrogenase Mutants from Anabaena sp. PCC 7120. Proteomics 19 (19), 1800332 (2019)

Murphy, B. J.; Klusch, N.; Langer, J. D.; Mills, D.; Yildiz, Ö.; Kühlbrandt, W.: Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F₁-F_o coupling. Science 364 (6446), eaaw9128, p. 1155 (2019)

Zakrzewska, S.; Mehdipour, A. R.; Malviya, V. N.; Nonaka, T.; Koepke, J.; Muenke, C.; Hausner, W.; Hummer, G.; Safarian, S.; Michel, H.: Inward-facing conformation of a multidrug resistance MATE family transporter. Proceedings of the National Academy of Sciences of the United States of America 116 (25), pp. 12275 - 12284 (2019)

Langebeck-Jensen, K.; Shahar, O. D.; Schuman, E. M.; Langer, J. D.; Soojin, R.: Larval Zebrafish Proteome Regulation in Response to an Environmental Challenge. Proteomics 19 (14), 1900028 (2019)

Huang, G.; Wagner, T.; Wodrich, M. D.; Ataka, K.; Bill, E.; Ermler, U.; Hu, X.; Shima, S.: The atomic-resolution crystal structure of activated [Fe]-hydrogenase. Nature Catalysis 2 (6), pp. 537 - 543 (2019)

Singh, S.; Akhter, M. S.; Dodt, J.; Volkers, P.; Reuter, A.; Reinhart, C.; Krettler, C.; Oldenburg, J.; Biswas, A.: Identification of Potential Novel Interacting Partners for Coagulation Factor XIII B (FXIII-B) Subunit, a Protein Associated with a Rare Bleeding Disorder. International Journal of Molecular Sciences 20 (11), 2682 (2019)

Willistein, M.; Bechtel, D. F.; Müller, C. S.; Demmer, U.; Heimann, L.; Kayastha, K.; Schünemann, V.; Pierik, A. J.; Ullmann, G. M.; Ermler, U. et al.; Boll, M.: Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactorsLow potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors. Nature Communications 10, 2074 (2019)

Watanabe, T.; Wagner, T.; Huang, G.; Kahnt, J.; Ataka, K.; Ermler, U.; Shima, S.: The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates. Angewandte Chemie International Edition in English 58 (11), pp. 3506 - 3510 (2019)