Crystal structure of cyanobacterial photosystem II at 3.0 A resolution: a closer look at the antenna system and the small membrane-intrinsic subunits. |
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Authors: | Frank Müh Thomas Renger Athina Zouni |
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Affiliation: | 1. International Centre for Quantum and Molecular Structures, College of Sciences, Shanghai University, Shanghai 200444, China;2. School of Mathematical and Physical Sciences, The University of Technology Sydney, Sydney, NSW 2007, Australia;3. Department of Biological Sciences, Brock University, St. Catharines, ON, Canada;4. Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA;5. School of Physical, Environmental and Mathematic Sciences, The University of New South Wales Canberra ACT 2600, Australia;6. Department of Applied Chemistry for Environment, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda, Hyogo 669-1337, Japan;7. Photonics Institute, TU Wien, Gusshausstrasse 27, 1040 Vienna, Austria;8. Department of Chemistry and Department of Physics, Kansas State University, Manhattan, KS 66505, USA;9. Zuse-Institute Berlin, Takustr. 7, 14195 Berlin, Germany;10. Institute of Physics, University of Tartu, Ravila 14c, 50411 Tartu, Estonia;11. Department of Chemistry, Ångström Laboratory, Uppsala University, Uppsala, Sweden;12. Institute of Theoretical Physics, Johannes Kepler University Linz, Altenberger Str. 69, 4040 Linz, Austria;13. Key Laboratory of Pesticide & Chemical Biology (CCNU), Ministry of Education, College of Chemistry, Central China Normal University, Wuhan 430079, China;14. Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences (CAS), Beijing 100190, China;15. Faculty of Science, Ibaraki University, Mito 310-8512, Japan;p. Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Nanxincun 20, Xiangshan, Beijing 100093, China;q. Department of Chemistry, Renmin University of, China;r. Institute of Molecular and Cell Biology, University of Tartu, Riia 23, 51010 Tartu, Estonia;s. Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia |
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Abstract: | Photosystem II (PSII) is a homodimeric protein-cofactor complex embedded in the thylakoid membrane that catalyses light-driven charge separation accompanied by the water splitting reaction during oxygenic photosynthesis. In the first part of this review, we describe the current state of the crystal structure at 3.0 A resolution of cyanobacterial PSII from Thermosynechococcus elongatus [B. Loll et al., Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II, Nature 438 (2005) 1040-1044] with emphasis on the core antenna subunits CP43 and CP47 and the small membrane-intrinsic subunits. The second part describes first the general theory of optical spectra and excitation energy transfer and how the parameters of the theory can be obtained from the structural data. Next, structure-function relationships are discussed that were identified from stationary and time-resolved experiments and simulations of optical spectra and energy transfer processes. |
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