2004 Fiscal Year Final Research Report Summary
Elucidation of the Molecular Mechanisms of Photosystem II Complex Based on Its Crystal Structure Analysis
| Project/Area Number |
14340257
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
植物生理
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| Research Institution | OKAYAMA UNIVERSITY (2003-2004)
The Institute of Physical and Chemical Research (2002) |
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Principal Investigator |
SHEN Jian-ren Okayama University, Faculty of Science, Department of Biology, Professor, 理学部, 教授 (60261161)
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| Co-Investigator(Kenkyū-buntansha) |
KAMIYA Nobuo RIKEN Harima Institute, Vice-Chief Researcher, 播磨研究所, 副主任研究員 (60152865)
IKEUCHI Masahiko University of Tokyo, Graduate School of Arts and Sciences, Professor, 大学院・総合文化研究科, 教授 (20159601)
ENAMI Isao Tokyo University of Science, Faculty of Science, Department of Biology, Professor, 理学研究科, 教授 (40084305)
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| Project Period (FY) |
2002 – 2004
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| Keywords | Photosynthesis / Photosystem II / Crystallization / Membrane Proteins / Protein Complexes / Crystallography / X-rays / Synchrotron Radiation |
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| Research Abstract |
Photosystem II (PSII) is a supra-molecular membrane-protein complex consisting of 14-17 membrane-spanning subunits and 3 membrane-peripheral (extrinsic) subunits with a total molecular mass of 350 kDa. This research aimed to analyze the crystal structure of PSII and, on the basis of this, to elucidate the molecular mechanisms of electron transfer, water-splitting and oxygen-evolving reactions taken place in PSII. For this purpose, we crystallized the PSII complex from a thermophilic cyanobacterium Thermosynechococcus vulcanus and analyzed its crystal structure at 3.7Å resolution in which, we assigned 70-80% residues of PSII large subunits CP47,CP43,D1,D2 based on the electron density maps of some residue's large side chains which were visible at the current resolution. We built the structures of all the 3 extrinsic proteins involved in oxygen evolution, of which, the structure of 12 kDa protein was reported for the first time. The whole structure contained in addition 14 trans-membrane helices, some of which were assigned to some low-molecular mass subunits including the α and β-subunits of cytochrome b559,and other helices were not identified. In the reaction center 4 chlorophylls, we identified that the "special dimer" PD1-PD2 has a shorter distance than those between them and the two "accessory chlorophylls", suggesting that the PSII reaction center is not a homogenous "tetramer". We assigned two β-carotenes between the region of D2 and cytochrome b559, thus implied that the secondary electron transfer pathway in PSII is from cytochrome b559 or ChlZD_2 via the two β-carotenes in series and then to ChlD_2,PD_2,PD_1. We also obtained the electron density for the Mn-cluster which is a Y-shaped or "3+1" model as reported previously. We further improved the PSII crystal resolution to 3.5Å, modified our original PSII structure model, and analyzed the PSII functions in more details based on the modified structure.
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[Journal Article] ATP-induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC.2003
Author(s)
Hayashi F., Suzuki H., Iwase R., Uzumaki T., Miyake A., Shen J.-R., Imada K., Furukawa Y., Yonekura K., Namba K., Ishiura M.
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Journal Title
Genes to Cells 8
Pages: 287-296
Description
「研究成果報告書概要(和文)」より
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[Journal Article] Comparison of binding and functional properties of two extrinsic components, cytochrome c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII.2003
Author(s)
Enami I., Iwai M., Akiyama A., Suzuki T., Okumura A., Katoh T., Tada O., Ohta H., Shen J.-R.
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Journal Title
Plant Cell Physiol. 44
Pages: 820-827
Description
「研究成果報告書概要(和文)」より
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[Journal Article] ATP-induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC2003
Author(s)
Hayashi F., Suzuki H., Iwase R., Uzumaki T., Miyake A., Shen J.-R., Imada K., Furukawa Y., Yonekura K., Namba K., Ishiura M.
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Journal Title
Genes to Cells 8
Pages: 287-296
Description
「研究成果報告書概要(欧文)」より
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