Publications

2018

  • Adam, S., and Bondar A.-N. (2018). Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin. PLoS One. 13(8), e0201298, doi: 10.1371/journal.pone.0201298.

  • Adam S., Knapp-Mohammady M., Yi J., and Bondar A-N. (2018). Revised CHARMM force-field parameters for iron-containing cofactors of photosystem II. J Comput Chem 39, 7-20.

  • Balke, J., Volz, P., Neumann, F., Brodwolf, R., Wolf, A., Pischon, H., Radbruch, M., Mundhenk, L., Gruber, A. D., Ma, N., and Alexiev, U. (2018). Visualizing Oxidative Cellular Stress Induced by Nanoparticles in the Subcytotoxic Range using Fluorescence Lifetime Imaging. Small 14 (23), doi: 10.1002/smll.201800310.

  • Baumann, T., Schmitt, F. J., Pelzer, A., Spiering, V. J., Freiherr von Sass, G. J., Friedrich, T., Budisa, N. (2018). Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence. J Vis Exp 134, e57017.

  • Daldrop, J. O., Kappler, J., Brunig, F. N., and Netz, R. R. (2018). Butane dihedral angle dynamics in water is dominated by internal friction. Proc Natl Acad Sci USA 115, 5169-5174.

  • Daldrop, J. O., Saita, M., Heyden, M., Lorenz-Fonfria, V. A., Heberle. J., and Netz, R. R. (2018). Orientation of non-spherical protonated water clusters revealed by infrared absorption dichroism. Nature Commun 9, 311.

  • Elgeti, M., Kazmin, R., Rose, A. S., Szczepek, M., Hildebrand, P. W., Bartl, F. J., Scheerer, P., and Hofmann, K. P. (2018). The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin. J Biol Chem 293, 4403-4410.

  • Elghobashi-Meinhardt, N., Phatak, P., Bondar, A.-N., Elstner, M., and Smith, J. C. (2018). Catalysis of ground state cis-trans isomerization of bacteriorhodopsin’s retinal chromophore by a hydrogen-bond network. Journal of membrane Biology (Topical Collection) 251:315-327, doi:10.1007/s00232-018-0027-x.

  • Geiger, M.-A., Jagtap, A.P., Kaushik, M., Sun, H., Stöppler, D., Sigurdsson, S.T., Corzilius, B., and Oschkinat, H. (2018). Efficiency of Water‐Soluble Nitroxide Biradicals for Dynamic Nuclear Polarization in Rotating Solids at 9.4 T: bcTol‐M and cyolyl‐TOTAPOL as New Polarizing Agents. Chemistry 24(51), doi: 10.1002/chem.201801251.

  • Ghane, T., Gorriz, R. F., Wrzalek, S., Volkenandt, S., Delatieh, F., Reidelbach, M., and Imhof, P. (2018) Hydrogen-Bonded Network and Water Dynamics in the D-channel of Cytochrome c Oxidase. The Journal of Membrane Biology 251, 299-314, doi: 10.1007/s00232-018-0019-x.

  • Grimm, C., Silapetere, A., Vogt, A., Bernal S., Yinth A., and Hegemann, P. (2018). Electrical properties, substrate specificity and optogenetic potential of the engineered light-driven sodium pump eKR2. Sci Rep 8, 9316.

  • Guerra, F., Siemers, M., Mielack, C., and Bondar, A.-N. (2018). Dynamics of Long-Distance Hydrogen-Bond Networks in Photosystem II. J Phys Chem B 122, 4625-4641.

  • Guo, Y., Wolff, F. E., Schapiro, I., Elstner, M., Marazzi, M. (2018). Different hydrogen bonding environments of the retinal protonated Schiff base control the photoisomerization in channelrhodopsin-2. Phys Chem Chem Phys 20, 27501-27509, doi: 10.1039/c8cp05210g.

  • Harris, A., Saita, M., Resler, T., Hughes-Visentin, A., Maia, R., Pranga-Sellnau, F., Bondar, A.-N., Heberle, J., and Brown, L. S. (2018). Molecular details of the unique mechanism of chloride transport by a cyanobacterial rhodopsin. Phys Chem Chem Phys 20, 3184-3199.

  • Hu, H.., Ataka, K., Menny, A., Fourati, Z., Sauguet, L., Corringer, P. J., Koehl, P., Heberle, J., Delarue, M. (2018). Electrostatics, proton sensor, and networks governing the gating transition in GLIC, a proton-gated pentameric ion channel. Proc Natl Acad Sci USA 115 (52), doi: 10.1073/pnas.1813378116.

  • Hussein, R., Ibrahim, M., Chatterjee, R., Coates, L., Muh, F., Yachandra, V. K., Yano, J., Kern, J., Dobbek, H., Zouni, A. (2018). Optimizing Crystal Size of Photosystem II by Macroseeding: Toward Neutron Protein Crystallography. Cryst Growth Des 18, 85-94.

  • Kern, J., Chatterjee, R., Young, I. D., Fuller, F. D., Lassalle, L., Ibrahim, M., Gul, S., Fransson, T., Brewster, A. S., Alonso-Mori, R., Hussein, R., Zhang, M., Douthit, L., de Lichtenberg, C., Cheah, M. H., Shevela, D., Wersig, J., Seuffert, I., Sokaras, D., Pastor, E., Weninger, C., Kroll, T., Sierra, R. G., Aller, P., Butryn, A., Orville, A. M., Liang, M., Batyuk, A., Koglin, J. E., Carbajo, S., Boutet, S., Moriarty, N. W., Holton, J. M., Dobbek, H., Adams, P. D., Bergmann, U., Sauter, N. K., Zouni, A., Messinger, J., Yano, J., and Yachandra, V. K. (2018). Structures of the intermediates of Kok's photosynthetic water oxidation clock. Nature 563, 421-425.

  • Mamatkulov, S. I., Rinne, K. F., Buchner, R., Netz, R. R., and Bonthuis, D. J. (2018). Water-separated ion pairs cause the slow dielectric mode of magnesium sulfate solutions. J Chem Phys 148, 222812.

  • Nogly, P., Weinert, T., James, D., Carbajo, S., Ozerov, D., Furrer, A., Gashi, D., Borin, V., Skopintsev, P., Jaeger, K., Nass, K., Bath, P., Bosman, R., Koglin, J., Seaberg, M., Lane, T., Kekilli, D., Brunle, S., Tanaka, T., Wu, W., Milne, C., White, T., Barty, A., Weierstall, U., Panneels, V., Nango, E., Iwata, S., Hunter, M., Schapiro, I., Schertler, G., Neutze, R., and Standfuss, J. (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science 361, 6398.

  • Oda, K., Vierock, J., Oishi, S., Rodriguez-Rozada, S., Taniguchi, R., Yamashita, K., Wiegert, J.S., Nishizawa, T., Hegemann, P., Nureki, O. (2018). Crystal structure of the red light-activated channelrhodopsin Chrimson. Nature Comm. 9(1):3949. doi: 10.1038/s41467-018-06421-9.

  • Pfitzner, E., Seki, H., Schlesinger, R., Ataka, K., and Heberle, J. (2018). Disc Antenna Enhanced Infrared Spectroscopy: From Self-Assembled Monolayers to Membrane Proteins. ACS Sens, 3 (5), pp 984–991, doi:10.1021/acssensors.8b00139.

  • Qureshi, B. M., Schmidt, A., Behrmann, E., Burger, J., Mielke, T., Spahn, C. M. T., Heck, M., and Scheerer, P. (2018). Mechanistic insights into the role of prenyl-binding protein PrBP/delta in membrane dissociation of phosphodiesterase 6. Nature Commun 9, 1-12.

  • Reidelbach, M., Weber, M., and Imhof, P. (2018). Prediction of perturbed proton transfer networks. Plos ONE. doi: org/10.1371/journal.pone.0207718.

  • Rossini, E., Bochevarov, A. D., and Knapp, E. W. (2018). Empirical Conversion of pKa Values between Different Solvents and Interpretation of the Parameters: Application to Water, Acetonitrile, Dimethyl Sulfoxide, and Methanol. ACS Omega 3, 1653-1662.

  • Saita, M., Pranga-Sellnau, F., Resler, T., Schlesinger, R., Heberle, J., and Lorenz-Fonfria, V. A. (2018). Photoexcitation of the P4(480) State Induces a Secondary Photocycle That Potentially Desensitizes Channelrhodopsin-2. J Am Chem Soc 140, 9899-9903.

  • Scheerer, P., Unger, E., and Tian, L. (2018). Protein structures guide the design of a much-needed tool for neuroscience. Nature 561, 312-313.

  • Scheib, U., Broser, M., Constantin, O. M., Yang, S.,Gao, S., Mukherjee, S., Stehfest, K., Nagel, G., Gee, C. E., and Hegemann, P. (2018). Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain. Nature Commun 9, 2046.

  • Schmidt, A., Sauthof, L., Szczepek, M., Lopez, M., Velázquez, F., Qureshi, B. M., Michael, N., Buhrke, D., Stevens, T., Kwiatkowski, D., von Stetten, D., Mroginski, M. A., Krauß, N., Lamparter, T. , Hildebrandt, P., and Scheerer, P. (2018). Structural snapshot of a bacterial phytochrome in its functional intermediate state. Nature Commun 9, 4912.

  • Schnedermann, C., Yang, X., Liebel, M., Spillane, K. M., Lugtenburg, J., Fernandez, I., Valentini, A., Schapiro, I., Olivucci, M., Kukura, P., Mathies, R. A. (2018). Evidence for a vibrational phase isotope effect on the photochemistry of vision. Nature Chemistry, 2018, 10, 449-455, doi: 10.1038/s41557-018-0014-y.

  • Schultz, B.-J., Mohrmann, H., Lórenz-Fonfría, V.A., and Heberle J. (2018). Protein dynamics observed by tunable mid-IR quantum cascade lasers across the time range from 10 ns to 1 s. Spectrochim Acta A 188, 666-674.

  • Schuth, N., Zaharieva, I., Chernev, P., Berggren, G., Anderlund, M., Styring, S., Dau, H., and Haumann, M. (2018). Kalpha X-ray Emission Spectroscopy on the Photosynthetic Oxygen-Evolving Complex Supports Manganese Oxidation and Water Binding in the S3 State. Inorg Chem 57,10424-10430.

  • Stöppler. D., Macpherson. A., Smith-Penzel, S., Basse, N., Lecomte, F., Deboves, H., Taylor, R.D., Norman, T., Porter, J., Waters, L.C., Westwood, M., Cossins, B., Cain, K., White, J., Griffin, R., Prosser, C., Kelm, S., Sullivan, A.H., Fox, D. 3rd, Carr, M.D., Henry, A., Taylor, R., Meier, B.H., Oschkinat, H., and Lawson, A.D. (2018). Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR. PLoS Biol. 16(5), doi: 10.1371/journal.pbio.2006192.

  • Sullivan, B., Archibald, R., Langan, P. S., Dobbek, H., Bommer, M., McFeeters, R. L., Coates, L., Wang, X., Gallmeier, F., Carpenter, J. M., Lynch, V., and Langan, P. (2018). Improving the accuracy and resolution of neutron crystallographic data by three-dimensional profile fitting of Bragg peaks in reciprocal space. Acta Crystallogr D Struct Biol 74, 1085-1095.

  • Song, C., Mroginski, M. A., Lang, C., Kopycki, J., Gartner, W., Matysik, J., and Hughes, J. (2018). 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function. Front Plant Sci 9, 498.

  • Wiebeler, Ch., Rao, A. G., Gärtner, W., and Schapiro, I. (2018). The Effective Conjugation Length is Responsible for the Red/Green Spectral Tuning in the Cyanobacteriochrome Slr1393g3. Angewandte Chemie 58(7), 1934-1938, doi: org/10.1002/anie.201810266.