The Wiley Prize in Biomedical Sciences is intended to recognize breakthrough research in pure or applied life science research that is distinguished by its excellence, originality and impact on our understanding of biological systems and processes. The award may recognize a specific contribution or series of contributions that demonstrate the nominee’s significant leadership in the development of research concepts or their clinical application. Particular emphasis will be placed on research that champions novel approaches and challenges accepted thinking in the biomedical sciences.
The ninth annual Wiley Prize in Biomedical Sciences was awarded jointly to Dr. Peter Hegemann, Professor of Molecular Biophysics, Humboldt University, Berlin; Dr. Georg Nagel, Professor of Molecular Plant Physiology, Department of Botany, University of Würzburg; and Dr. Ernst Bamberg, Professor and Director of the Dept of Biophysical Chemistry, Max Planck Institute for Biophysics, Frankfurt, Germany for their discovery of channelrhodopsins, a family of light-activated ion channels. The discovery has greatly enlarged and strengthened the new field of optogenetics. Channelrhodopsins also provide a high potential for biomedical applications such as the recovery of vision and optical deep brain stimulation for treatment of Parkinson’s and other diseases, instead of the more invasive electrode-based treatments.
Dr. Ernst Bamberg's Biography
Ph.D. Physical Chemistry, University of Basel, 1971
Habilitation, University of Konstanz, 1976
Heisenberg fellow, 1979
Group leader, independent research group,
Max-Planck-Institute of Biophysics, Frankfurt, 1983
Apl. Professor, University of Frankfurt, 1988
Full Professor, Biophysical Chemistry, University of Frankfurt, 1993-2009
Director, Department of Biophysical Chemistry since 1993
Dr. Ernst Bamberg's Research
Retinal proteins light-gated ion channels and light-driven ion pumps and their application in neuro and cell biology
Light-gated ion channels. Recently, a novel class of ion channels, the light-gated channelrhodopsins (ChR1 and ChR2) has been discovered. They possess a seven transmembrane helix motif similar to that of other microbial rhodopsins and were investigated in part by electrophysiological methods in heterologously expressing cells (Nagel et al, 2002, 2003, 2005b). These channels represent a long sought-after and unique tool for neurobiological applications (Fig. 1) because they allow the light-induced depolarization of cells. This was demonstrated in nerve cells as well as in excitable cells in transgenic animals by induction of light dependent behavior as well as restoration of light reactions in a blind mouse. Meanwhile, ChR2 has found a worldwide application in many neurobiologically oriented laboratories. The mechanism of these ion channels is still unknown. Therefore, the function and structure of these membrane proteins need to be investigated in detail. By determining simultaneously the photocycle and the kinetics of the channel current the spectroscopic intermediate of the photocycle, which represents the open state of the channel, was identified (Bamann et al, 2008). By noise analysis the single channel conductance was determined to 35 fS. In the same paper it was demonstrated that ChR2 acts as a leaky light-driven proton pump (Feldbauer et al, 2009). In the future we are searching to construct channelrhodopsins with higher light sensitivity and larger single channel conductance, which would be desirable for neurobiological applications. New molecules are under construction which allow the activation and inactivation of nerve cells at different wavelengths with high spatial precision.
Structural analysis by 2D and 3D crystallization is under study with the Departments of Structural Biology and Molecular Membrane Biology.
The group is a member of an international consortium on the recovery of vision by use of ChR2 and of the Bernstein Center for Computational Neuroscience Göttingen for network analysis.
Yonehara,K., Balint,K., Noda,M., Nagel,G., Bamberg,E. and Roska,B.: Spatially asymmetric reorganization of inhibition establishes a motion-sensitive circuit. Nature 469, 407-410 (2011).
Bamann, C., Gueta, R., Kleinlogel, S., Nagel, G. and Bamberg, E.: Structural Guidance of the Photocycle of Channelrhodopsin-2 by an Interhelical Hydrogen Bond. Biochemistry 49 (2), 267-278 (2010).
Bamann, C., Nagel, G. and Bamberg, E.: Microbial rhodopsins in the spotlight. Curr. Opin. Neurobiol. 20, 610-616 (2010).
Carpaneto, A., Koepsell, H., Bamberg, E., Hedrich, R. and Geiger, D.: Sucrose- and H+-Dependent Charge Movements Associated with the Gating of Sucrose Transporter ZmSUT1. PLoS One 5, e12605 (2010).
Hoffmann, J., Aslimovska, L., Bamann, C., Glaubitz, C., Bamberg, E. and Brutschy, B.: Studying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channel. Phys. Chem. Chem. Phys. 12, 3480-3485 (2010).
Hofmann, B., Maybeck, V., Eick, S., Meffert, S., Ingebrandt, S., Wood, P., Bamberg E. and Offenhäusser, A.: Light induced stimulation and delay of cardiac activity. Lap Chip 10, 2588-2596 (2010).
Nack, M., Radu, I., Gossing, M., Bamann, C., Bamberg, E., Fischer von Mollard, G. and Heberle, J.: The DC gate in Channelrhodopsin-2: crucial hydrogen bonding interaction between C128 and D156. Photochem. Photobiol. Sci. 9, 194-198 (2010).
Verhoefen, M.-K., Bamann, C., Blöcher, R., Förster, U., Bamberg, E. and Wachtveitl, J: The Photocycle of Channelrhodopsin-2: Ultrafast Reaction Dynamics and Subsequent Reaction Steps. ChemPhysChem 11, 3113-3122 (2010).
Zimmermann, U., Rüger, S., Shapira, O., Westhoff, M., Wegner, L.H., Reuss, R., Gessner, P., Zimmermann, G., Israeli, Y., Zhou, A., Schwartz, A., Bamberg, E. and Zimmermann, D.: Effects of environmental parameters and irrigation on the turgor pressure of banana plants measured using the non-invasive, online monitoring leaf patch clamp pressure probe. Plant Biology 12, 424-436 (2010).
Feldbauer, K., Zimmermann, D., Pintschovius, V., Spitz, J., Bamann, C., Bamberg, E.: Channelrhodopsin-2 is a leaky proton pump. Proc. Natl. Acad. Sci. 106 12317-12322 (2009).
Bamann,C., Kirsch,T., Nagel,G.Bamberg,E. (2008) Spectral characteristics of the photocycle of channelrhodopsin-2 and its implication for channel function. J.Mol. Biol. 375,686-694
Dempski,R.,Lustig,J.,Friedrich,T.Bamberg,E. (2008) Structural Arrangement and Conformational Dynamics of the Gamma Subunit of the Na+/K+ ATPase. Biochemistry 47,257-266
Kalmbach,R., Chizhov,I.,Schumacher,M.,Friedrich,T.,Bamberg,E. Engelhard,M. (2007) Functional Cell-free Synthesis of a Seven Helix Membrane Protein: In situ Insertion of Bacteriorhodopsin into Liposomes. J.Mol.Biol 371,639-648
Nagel,G.,Gottschalk,A., Deisseroth,K. (2007) Multimodal fast optical interrogation of neural circuits.
Boyden, E.S., Zhang,F., Bamberg,E., Nagel,G., Deisseroth,K. (2005) Millisecond-timescale, genetically targeted optical control of neural activity. Nature Neuroscience 8(9):1263-1268.
Dempski, R.E., Friedrich, T.,Bamberg, E. (2005) The b subunit of the Na+/K+-ATPase follows the conformational state of the holoenzyme. Journal of General Physiology 125, 505-520).
Nagel, G., Szellas, T., Huhn, W., Kateriya, S., Adeishvili, N., Berthold, P., Ollig, D., Hegemann, P., Bamberg, E. (2003). Channelrhodopsin-2, a directly Light-gated Cation-selective Membrane Channel.
Proc. Natl. Acad. Sci. 100, 13940-13945
Geibel, S., Kaplan, J.H., Bamberg, E., Friedrich, T. (2003).Conformational Dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry. Proc. Natl. Acad. Sci. 100, 964-969
Nagel, G., Ollig, D., Fuhrmann, M., Kateriya, S., Musti, A.-M., Bamberg, E., Hegemann, P. (2002) Channelrhodopsin-1, A Light-Gated Proton Channel in Green Algae. Science 296, 2395-2398