Publikationen der Emeritus Gruppe für Biophysikalische Chemie

Okhrimenko, I. S.; Kovalev, K.; Petrovskaya, L. E.; Ilyinsky, N. S.; Alekseev, A. A.; Marin, E.; Rokitskaya, T. I.; Antonenko, Y. N.; Siletsky, S. A.; Popov, P. A. et al.; Zagryadskaya, Y. A.; Soloviov, D. V.; Chizhov, I. V.; Zabelskii, D. V.; Ryzhykau, Y. L.; Vlasov, A. V.; Kuklin, A. I.; Bogorodskiy, A. O.; Mikhailov, A. E.; Sidorov, D. V.; Bukhalovich, S.; Tsybrov, F.; Bukhdruker, S.; Vlasova, A. D.; Borshchevskiy, V. I.; Dolgikh, D. A.; Kirpichnikov, M. P.; Bamberg, E.; Gordeliy, V. I.: Mirror proteorhodopsins. Communications Chemistry 6, 88 (2023)

Gorriti, M. F.; Bamann, C.; Alonso-Reyes, D. G.; Wood, P. G.; Bamberg, E.; Farías, M. E.; Gärtner, W.; Albarracín, V. H.: Functional characterization of xanthorhodopsin in Salinivibrio socompensis, a novel halophile isolated from modern stromatolites. Photochemical & Photobiological Sciences (2023)

Astashkin, R.; Kovalev, K.; Bukhdruker, S.; Vaganova, S.; Kuzmin, A.; Alekseev, A.; Balandin, T.; Zabelskii, D.; Gushchin, I.; Royant, A. et al.; Volkov, D.; Bourenkov, G.; Koonin, E.; Engelhard, M.; Bamberg, E.; Gordeliy, V.: Structural insights into light-driven anion pumping in cyanobacteria. Nature Communications 13, 6460 (2022)

Borshchevskiy, V.; Kovalev, K.; Round, E.; Efremov, R.; Astashkin, R.; Bourenkov, G.; Bratanov, D.; Balandin, T.; Chizhov, I.; Baeken, C. et al.; Gushchin, I.; Kuzmin, A.; Alekseev, A.; Rogachev, A.; Willbold, D.; Engelhard, M.; Bamberg, E.; Büldt, G.; Gordeliy, V.: True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nature Structural and Molecular Biology 29 (5), S. 440 - 450 (2022)

Weissbecker, J.; Boumrifak, C.; Breyer, M.; Wießalla, T.; Shevchenko, V.; Mager, T.; Slavov, C.; Alekseev , A.; Kovalev, K.; Gordeliy , V. et al.; Bamberg, E.; Wachtveitl, J.: The voltage dependent sidedness of the reprotonation of the retinal Schiff base determines the unique inward pumping of Xenorhodopsin. Angewandte Chemie, International Edition in English 60 (42), S. 23010 - 23017 (2021)

Schumacher, M.; Klare, J. P.; Bamann, C.; Steinhoff, H.-J.: DEER Spectroscopy of Channelrhodopsin-2 Helix B Movements in Trapped Photocycle Intermediates. Applied Magnetic Resonance (2021)

Becker-Baldus, J.; Leeder, A.; Brown, L. J.; Brown, R. C. D.; Bamann, C.; Glaubitz, C.: The Desensitized Channelrhodopsin-2 Photointermediate Contains 13 -cis, 15 -syn Retinal Schiff Base. Angewandte Chemie, International Edition in English 60 (30), S. 16442 - 16447 (2021)

Zabelskii, D.; Dmitrieva, N.; Volkov, O.; Shevchenko, V.; Kovalev, K.; Balandin, T.; Soloviov, D.; Astashkin, R.; Zinovev, E.; Alekseev, A. et al.; Round, E.; Polovinkin, V.; Chizhov, I.; Rogachev, A.; Okhrimenko, I.; Borshchevskiy, V.; Chupin, V.; Büldt, G.; Yutin, N.; Bamberg, E.; Koonin, E.; Gordeliy, V.: Structure-based insights into evolution of rhodopsins. Communications Biology 4 (1), 821 (2021)

Jakdetchai, O.; Eberhardt, P.; Asido, M.; Kaur, J.; Kriebel, C. N.; Mao, J.; Leeder, A. J.; Brown, L. J.; Brown, R. C. D.; Becker-Baldus, J. et al.; Bamann, C.; Wachtveitl, J.; Glaubitz, C.: Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR. Science Advances 7 (11), eabf4213 (2021)

Eberhardt, P.; Slavov, C.; Sörmann, J.; Bamann, C.; Braun, M.; Wachtveitl, J.: Temperature Dependence of the Krokinobacter rhodopsin 2 Kinetics. Biophysical Journal (Annual Meeting Abstracts) 120 (3), S. 568 - 575 (2021)

Zabelskii, D.; Alekseev, A.; Kovalev, K.; Rankovic, V.; Balandin, T.; Soloviov, D.; Bratanov, D.; Savelyeva, E.; Podolyak, E.; Volkov, D. et al.; Vaganova, S.; Astashkin, R.; Chizhov, I.; Yutin, N.; Rulev, M.; Popov, A.; Eria-Oliveira, A.-S.; Rokitskaya, T.; Mager, T.; Antonenko, Y.; Rosselli, R.; Armeev, G.; Shaitan, K.; Vivaudou, M.; Büldt, G.; Rogachev, A.; Rodriguez-Valera, F.; Kirpichnikov, M.; Moser, T.; Offenhäusser, A.; Willbold, D.; Koonin, E.; Bamberg, E.; Gordeliy, V.: Viral rhodopsins 1 are an unique family of light-gated cation channels. Nature Communications 11, 5707 (2020)

Reyer, A.; Häßler, M.; Scherzer, S.; Huang, S.; Pedersen, J. T.; Al-Rascheid, K. A. S.; Bamberg, E.; Palmgren, M.; Dreyer, I.; Nagel, G. et al.; Hedrich, R.; Becker, D.: Channelrhodopsin-mediated optogenetics highlights a central role of depolarization-dependent plant proton pumps. Proceedings of the National Academy of Sciences of the United States of America 117 (34), S. 20920 - 20925 (2020)

Kovalev, K.; Astashkin, R.; Gushchin, I.; Orekhov, P.; Volkov, D.; Zinovev, E.; Marin, E.; Rulev, M.; Alekseev, A.; Royant, A. et al.; Carpentier, P.; Vaganova, S.; Zabelskii, D.; Baeken, C.; Sergeev, I.; Balandin, T.; Bourenkov, G.; Carpena, X.; Boer, R.; Maliar, N.; Borshchevskiy, V.; Büldt, G.; Bamberg, E.; Gordeliy, V.: Molecular mechanism of light-driven sodium pumping. Nature Communications 11, 2137 (2020)

Kovalev, K.; Volkov, D.; Astashkin, R.; Alekseev, A.; Gushchin, I.; Haro-Moreno, J. M.; Chizhov, I.; Siletsky, S.; Mamedov, M.; Rogachev, A. et al.; Balandin, T.; Borshchevskiy, V.; Popov, A.; Bourenkov, G.; Bamberg, E.; Rodriguez-Valera, F.; Büldt, G.; Gordeliy, V.: High-resolution structural insights into the heliorhodopsin family. Proceedings of the National Academy of Sciences of the United States of America 117 (8), S. 4131 - 4141 (2020)

Ehrenberg, D.; Krause, N.; Saita, M.; Bamann, C.; Kar, R. K.; Hoffmann, K.; Heinrich, D.; Schapiro, I.; Heberle, J.; Schlesinger, R.: Atomistic Insight into the Role of Threonine 127 in the Functional Mechanism of Channelrhodopsin-2. Applied Sciences 9 (22), 4905 (2019)

Bratanov, D.; Kovalev, K.; Machtens, J.-P.; Astashkin, R.; Chizhov, I.; Soloviov, D.; Volkov, D.; Polovinkin, V.; Zabelskii, D.; Mager, T. et al.; Gushchin, I.; Rokitskaya, T.; Antonenko, Y.; Alekseev, A.; Shevchenko, V.; Yutin, N.; Rosselli, R.; Baeken, C.; Borshchevskiy, V.; Bourenkov, G.; Popov, A.; Balandin, T.; Büldt, G.; Manstein, D. J.; Rodriguez-Valera, F.; Fahlke, C.; Bamberg, E.; Koonin, E.; Gordeliy, V.: Unique structure and function of viral rhodopsins. Nature Communications 10, 4939 (2019)

Kovalev, K.; Polovinkin, V.; Gushchin, I.; Alekseev, A.; Shevchenko, V.; Borshchevskiy, V.; Astashkin, R.; Balandin, T.; Bratanov, D.; Vaganova, S. et al.; Popov, A.; Chupin, V.; Büldt, G.; Bamberg, E.; Gordeliy, V.: Structure and mechanisms of sodium-pumping KR2 rhodopsin. Science Advances 5, eaav2671 (2019)

Kaur, J.; Kriebel, C. N.; Eberhardt, P.; Jakdetchai, O.; Leeder, A. J.; Weber, I.; Brown, L. J.; Brown, R. C.D.; Becker-Baldus, J.; Bamann, C. et al.; Wachtveitl, J.; Glaubitz, C.: Solid-state NMR analysis of the sodium pump Krokinobacter rhodopsin 2 and its H30A mutant. Journal of Structural Biology 206 (1), S. 55 - 65 (2019)

Vinayagam, D.; Mager, T.; Apelbaum, A.; Bothe, A.; Merino, F.; Hofnagel, O.; Gatsogiannis, C.; Raunser, S.: Electron cryo-microscopy structure of the canonical TRPC4 ion channel. eLife 7, e36615 (2018)

Mager, T. M.-H.; Lopez de la Morena, D.; Senn, V.; Schlotte, J.; D´Errico, A.; Feldbauer, K.; Wrobel, C.; Jung, S.; Bodensiek, K.; Rankovic, V. et al.; Browne, L.; Huet, A.; Jüttner, J.; Wood, P. G.; Letzkus, J.; Moser, T.; Bamberg, E.: High frequency neural spiking and auditory signaling by ultrafast red-shifted optogenetics. Nature Communications 9, 1750 (2018)