Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Logo for

Science 328 (5978): 630-633

Copyright © 2010 by the American Association for the Advancement of Science

Light-Induced Structural Changes in a Photosynthetic Reaction Center Caught by Laue Diffraction

Annemarie B. Wöhri,1,* Gergely Katona,2 Linda C. Johansson,2 Emelie Fritz,2 Erik Malmerberg,2 Magnus Andersson,1 Jonathan Vincent,3 Mattias Eklund,3 Marco Cammarata,4 Michael Wulff,4,{dagger} Jan Davidsson,3 Gerrit Groenhof,5 Richard Neutze2,{ddagger}

Abstract: Photosynthetic reaction centers convert the energy content of light into a transmembrane potential difference and so provide the major pathway for energy input into the biosphere. We applied time-resolved Laue diffraction to study light-induced conformational changes in the photosynthetic reaction center complex of Blastochloris viridis. The side chain of TyrL162, which lies adjacent to the special pair of bacteriochlorophyll molecules that are photooxidized in the primary light conversion event of photosynthesis, was observed to move 1.3 angstroms closer to the special pair after photoactivation. Free energy calculations suggest that this movement results from the deprotonation of this conserved tyrosine residue and provides a mechanism for stabilizing the primary charge separation reactions of photosynthesis.

1 Department of Chemical and Biological Engineering, Chalmers University of Technology, Box 462, SE-40530 Göteborg, Sweden.
2 Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, SE-40530 Göteborg, Sweden.
3 Department of Photochemistry and Molecular Science, Uppsala University, Box 523, SE-75120 Uppsala, Sweden.
4 European Synchrotron Radiation Facility, BP 220, Grenoble Cedex 38043, France.
5 Computational Biomolecular Chemistry Group, Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany.

* Present address: AstraZeneca Research and Development, Cell, Protein, and Structural Sciences, SE 43183 Mölndal, Sweden.

{dagger} Present address: SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.

{ddagger} To whom correspondence should be addressed. E-mail: Richard.Neutze{at}chem.gu.se


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Carboxylate Shifts Steer Interquinone Electron Transfer in Photosynthesis.
P. Chernev, I. Zaharieva, H. Dau, and M. Haumann (2011)
J. Biol. Chem. 286, 5368-5374
   Abstract »    Full Text »    PDF »
The Catalytic Aspartate Is Protonated in the Michaelis Complex Formed between Trypsin and an in Vitro Evolved Substrate-like Inhibitor: A REFINED MECHANISM OF SERINE PROTEASE ACTION.
W. Y. Wahlgren, G. Pal, J. Kardos, P. Porrogi, B. Szenthe, A. Patthy, L. Graf, and G. Katona (2011)
J. Biol. Chem. 286, 3587-3596
   Abstract »    Full Text »    PDF »
Macromolecular crystallography at synchrotron radiation sources: current status and future developments.
E. M. H. Duke and L. N. Johnson (2010)
Proc R Soc A 466, 3421-3452
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882