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Publications

2022

  • Allgower, F., Gamiz-Hernandez, A.P., Rutherford, A.W. and Kaila, V.R.I. (2022). Molecular Principles of Redox-Coupled Protonation Dynamics in Photosystem II. J Am Chem Soc, 144, 16: 7171-7180. doi: 10.1021/jacs.1c13041

  • Ataka, K., Baumann, A., Chen, J.L., Redlich, A., Heberle, J. and Schlesinger, R. (2022). Monitoring the Progression of Cell-Free Expression of Microbial Rhodopsins by Surface Enhanced IR Spectroscopy: Resolving a Branch Point for Successful/Unsuccessful Folding. Front Mol Biosci, 9, 929285. doi: 10.3389/fmolb.2022.929285.

  • Baidukova, O., Oppermann, J., Kelterborn, S., Fernandez Lahore, R.G., Schumacher, D., Evers, H., Kamrani, Y.Y. and Hegemann, P. (2022). Gating and ion selectivity of Channelrhodopsins are critical for photo-activated orientation of Chlamydomonas as shown by in vivo point mutation. Nat Commun, 13, 1: 7253. doi: 10.1038/s41467-022-35018-6.

  • Baserga, F., Vorkas, A., Crea, F., Schubert, L., Chen, J.-L., Redlich, A., La Greca, M., Storm, J., Oldemeyer, S., Hoffmann, K., Schlesinger, R. and Heberle, J. (2022). Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy. Front Mol Biosci, 9. doi: 10.3389/fmolb.2022.915328.

  • Bondar, A.N. (2022). Graphs of Hydrogen-Bond Networks to Dissect Protein Conformational Dynamics. J Phys Chem B, 126, 22: 3973-3984. doi: 10.1021/acs.jpcb.2c00200.

  • Bondar, A.N. (2022). Interplay between local protein interactions and water bridging of a proton antenna carboxylate cluster. Biochim Biophys Acta Biomembr, 1864, 12: 184052. doi: 10.1016/j.bbamem.2022.184052.

  • Brünig, F.N., Daldrop, J.O. and Netz, R.R. (2022). Pair-Reaction Dynamics in Water: Competition of Memory, Potential Shape, and Inertial Effects. J Phys Chem B. doi: 10.1021/acs.jpcb.2c05923.

  • Brünig, F.N., Geburtig, O., Canal, A.V., Kappler, J. and Netz, R.R. (2022). Time-Dependent Friction Effects on Vibrational Infrared Frequencies and Line Shapes of Liquid Water. J Phys Chem B, 126, 7: 1579-1589. doi: 10.1021/acs.jpcb.1c09481.

  • Brünig, F.N., Hillmann, P., Kim, W.K., Daldrop, J.O. and Netz, R.R. (2022). Proton-transfer spectroscopy beyond the normal-mode scenario. J Chem Phys, 157, 17: 174116. doi: 10.1063/5.0116686.
  • Brünig, F.N., Netz, R.R. and Kappler, J. (2022). Barrier-crossing times for different non-Markovian friction in well and barrier: A numerical study. Phys Rev E, 106, 4: 044133. doi: 10.1103/PhysRevE.106.044133.

  • Brünig, F.N., Rammler, M., Adams, E.M., Havenith, M. and Netz, R.R. (2022). Spectral signatures of excess-proton waiting and transfer-path dynamics in aqueous hydrochloric acid solutions. Nat Commun, 13, 1: 4210. doi: 10.1038/s41467-022-31700-x.

  • Crea, F., Vorkas, A., Redlich, A., Cruz, R., Shi, C., Trauner, D., Lange, A., Schlesinger, R. and Heberle, J. (2022). Photoactivation of a Mechanosensitive Channel. Front Mol Biosci. doi: 10.3389/fmolb.2022.905306

  • Emiliani, V., Entcheva, E., Hedrich, R., Hegemann, P., Konrad, K.R., Lüscher, C., Mahn, M., Pan, Z.-H., Sims, R.R., Vierock, J. and Yizhar, O. (2022). Optogenetics for light control of biological systems. Nat Rev Methods Primers, 2, 1: 55. doi: 10.1038/s43586-022-00136-4.

  • Filiba, O., Borin, V.A. and Schapiro, I. (2022). The involvement of triplet states in the isomerization of retinaloids. Phys Chem Chem Phys. doi: 10.1039/D2CP03791B.

  • Golub, M., Gatcke, J., Subramanian, S., Kolsch, A., Darwish, T., Howard, J.K., Feoktystov, A., Matsarskaia, O., Martel, A., Porcar, L., Zouni, A. and Pieper, J. (2022). "Invisible" Detergents Enable a Reliable Determination of Solution Structures of Native Photosystems by Small-Angle Neutron Scattering. J Phys Chem B, 126, 15: 2824-2833. doi: 10.1021/acs.jpcb.2c01591

  • Heyne, K. (2022). Impact of Ultrafast Electric Field Changes on Photoreceptor Protein Dynamics. J Phys Chem B, 126, 3: 581-587. doi: 10.1021/acs.jpcb.1c08131

  • Karathanou, K., Lazaratos, M., Bertalan, E., Siemers, M. and Bondar, A.N. (2022). Conformational coupling and proton binding with dynamic hydrogen-bond networks. Biophys J, 121, 3: 170a. doi: 10.1016/j.bpj.2021.11.1886.

  • La Greca, M., Chen, J.L., Schubert, L., Kozuch, J., Berneiser, T., Terpitz, U., Heberle, J. and Schlesinger, R. (2022). The Photoreaction of the Proton-Pumping Rhodopsin 1 From the Maize Pathogenic Basidiomycete Ustilago maydis. Front Mol Biosci, 9, 826990. doi: 10.3389/fmolb.2022.826990

  • Lazaratos, M., Siemers, M., Brown, L.S. and Bondar, A.N. (2022). Conserved hydrogen-bond motifs of membrane transporters and receptors. Biochim Biophys Acta Biomembr, 1864, 6: 183896. doi: 10.1016/j.bbamem.2022.183896

  • Liese, S., Schlaich, A. and Netz, R.R. (2022). Dielectric constant of aqueous solutions of proteins and organic polymers from molecular dynamics simulations. J Chem Phys, 156, 22: 224902. doi: 10.1063/5.0089397.

  • Lopez, M.F., Dahl, M., Escobar, F.V., Bonomi, H.R., Kraskov, A., Michael, N., Mroginski, M.A., Scheerer, P. and Hildebrandt, P. (2022). Photoinduced reaction mechanisms in prototypical and bathy phytochromes. Phys Chem Chem Phys, 24, 19: 11967-11978. doi: 10.1039/d2cp00020b.

  • Mous, S., Gotthard, G., Ehrenberg, D., Sen, S., Weinert, T., Johnson, P.J.M., James, D., Nass, K., Furrer, A., Kekilli, D., Ma, P., Brunle, S., Casadei, C.M., Martiel, I., Dworkowski, F., Gashi, D., Skopintsev, P., Wranik, M., Knopp, G., Panepucci, E., Panneels, V., Cirelli, C., Ozerov, D., Schertler, G.F.X., Wang, M., Milne, C., Standfuss, J., Schapiro, I., Heberle, J. and Nogly, P. (2022). Dynamics and mechanism of a light-driven chloride pump. Science, 375, 6583: 845-851. doi: 10.1126/science.abj6663.

  • Nagano, S., Sadeghi, M., Balke, J., Fleck, M., Heckmann, N., Psakis, G. and Alexiev, U. (2022). Improved fluorescent phytochromes for in situ imaging. Sci Rep, 12, 1: 5587. doi: 10.1038/s41598-022-09169-x.

  • Oliver, N., Avramov, A.P., Nurnberg, D.J., Dau, H. and Burnap, R.L. (2022). From manganese oxidation to water oxidation: assembly and evolution of the water-splitting complex in photosystem II. Photosynth Res, 152, 2: 107-133. doi: 10.1007/s11120-022-00912-z.

  • Palombo, R., Barneschi, L., Pedraza-González, L., Padula, D., Schapiro, I. and Olivucci, M. (2022). Retinal chromophore charge delocalization and confinement explain the extreme photophysics of Neorhodopsin. Nat Commun, 13, 1: 6652. doi: 10.1038/s41467-022-33953-y.

  • Rao, A.G. and Schapiro, I. (2022). Photoisomerization of phytochrome chromophore models: an XMS-CASPT2 study. Phys Chem Chem Phys. doi: 10.1039/D2CP04249E.

  • Rodriguez-Rozada, S., Wietek, J., Tenedini, F., Sauter, K., Dhiman, N., Hegemann, P., Soba, P. and Wiegert, J.S. (2022). Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing. Commun Biol, 5, 1: 687. doi: 10.1038/s42003-022-03636-x.

  • Sadeghi, M., Balke, J., Rafaluk-Mohr, T. and Alexiev, U. (2022). Long-Distance Protonation-Conformation Coupling in Phytochrome Species. Molecules, 27, 23: 8395. doi: 10.3390/molecules27238395.

  • Saura, P., Riepl, D., Frey, D.M., Wikström, M. and Kaila, V.R.I. (2022). Electric fields control water-gated proton transfer in cytochrome c oxidase. PNAS, 119, 38. doi: 10.1073/pnas.2207761119.

  • Schubert, L., Langner, P., Ehrenberg, D., Lorenz-Fonfria, V.A. and Heberle, J. (2022). Protein conformational changes and protonation dynamics probed by a single shot using quantum-cascade-laser-based IR spectroscopy. J Chem Phys, 156, 20: 204201. doi: 10.1063/5.0088526.

  • Silapetere, A., Hwang, S., Hontani, Y., Fernandez Lahore, R.G., Balke, J., Escobar, F.V., Tros, M., Konold, P.E., Matis, R., Croce, R., Walla, P.J., Hildebrandt, P., Alexiev, U., Kennis, J.T.M., Sun, H., Utesch, T. and Hegemann, P. (2022). QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins. Nat Commun, 13, 1: 5501. doi: 10.1038/s41467-022-33084-4.

  • Simon, P.S., Makita, H., Bogacz, I., Fuller, F., Bhowmick, A., Hussein, R., Ibrahim, M., Zhang, M., Chatterjee, R., Cheah, M.H., Chernev, P., Doyle, M.D., Brewster, A.S., Alonso-Mori, R., Sauter, N.K., Bergmann, U., Dobbek, H., Zouni, A., Messinger, J., Kern, J., Yachandra, V.K. and Yano, J. (2022). Capturing the sequence of events during the water oxidation reaction in photosynthesis using XFELs. FEBS Lett. doi: 10.1002/1873-3468.14527.

  • Viola, S., Roseby, W., Santabarbara, S., Nurnberg, D., Assuncao, R., Dau, H., Selles, J., Boussac, A., Fantuzzi, A. and Rutherford, A.W. (2022). Impact of energy limitations on function and resilience in long-wavelength Photosystem II. Elife, 11. doi: 10.7554/eLife.79890.

  • Walter, M., Schubert, L., Heberle, J., Schlesinger, R. and Losi, A. (2022). Time-resolved photoacoustics of channelrhodopsins: early energetics and light-driven volume changes. Photochem Photobiol Sci. doi: 10.1007/s43630-022-00327-8.

  • Weaver, J.B., Kozuch, J., Kirsh, J.M. and Boxer, S.G. (2022). Nitrile Infrared Intensities Characterize Electric Fields and Hydrogen Bonding in Protic, Aprotic, and Protein Environments. J Am Chem Soc, 144, 17: 7562-7567. doi: 10.1021/jacs.2c00675.

  • Yaguchi, M., Jia, X., Schlesinger, R., Jiang, X., Ataka, K. and Heberle, J. (2022). Near-Infrared Activation of Sensory Rhodopsin II Mediated by NIR-to-Blue Upconversion Nanoparticles. Front Mol Biosci, 8, 782688. doi: 10.3389/fmolb.2021.782688.

  • Yang, Y., Stensitzki, T., Sauthof, L., Schmidt, A., Piwowarski, P., Velazquez Escobar, F., Michael, N., Nguyen, A.D., Szczepek, M., Brünig, F.N., Netz, R.R., Mroginski, M.A., Adam, S., Bartl, F., Schapiro, I., Hildebrandt, P., Scheerer, P. and Heyne, K. (2022). Ultrafast proton-coupled isomerization in the phototransformation of phytochrome. Nat Chem. doi: 10.1038/s41557-022-00944-x.

  • Zahn, C., Stensitzki, T. and Heyne, K. (2022). Femtosecond anisotropy excitation spectroscopy to disentangle the Qx and Qy absorption in chlorophyll a. Chem Sci, 13, 42: 12426-12432. doi: 10.1039/D2SC03538C.

  • Zheng, C., Mao, Y., Kozuch, J., Atsango, A.O., Ji, Z., Markland, T.E. and Boxer, S.G. (2022). A two-directional vibrational probe reveals different electric field orientations in solution and an enzyme active site. Nat Chem. doi: 10.1038/s41557-022-00937-w.