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

Author:

Wöhri Annemarie B.1,Katona Gergely2,Johansson Linda C.2,Fritz Emelie2,Malmerberg Erik2,Andersson Magnus1,Vincent Jonathan3,Eklund Mattias3,Cammarata Marco4,Wulff Michael4,Davidsson Jan3,Groenhof Gerrit5,Neutze Richard2

Affiliation:

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.

Abstract

Light Structures Absorption of light by photosynthetic reaction centers causes structural changes and triggers a series of electron transfer reactions, resulting in a transmembrane potential difference that can be used to drive the subsequent chemistry. The initial electron transfer generates a charge-separated state that must be stabilized to prevent dissipation of energy through recombination. Wöhri et al. (p. 630 ) have used time-resolved Laue diffraction crystallography to observe light-induced conformational changes that occur within milliseconds of photooxidation of the dimer of bacteriochlorophyll molecules, known as the “special pair,” in the photosynthetic reaction center of Blastochloris viridis . Stabilization appears to occur because of the deprotonation of a conserved tyrosine residue that moves closer to the special pair.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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