| Project/Area Number |
05640728
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理
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| Research Institution | Kanazawa University |
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Principal Investigator |
HOSHINA Satoshi Kanazawa University, Faculty of Science Research Associate, 理学部, 助手 (50019486)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1994: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1993: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | alpha-helix / Amino acid sequence / Femtosecond spectroscopy / Photoinhibition / Photosystem I / Plastocyanin / Reaction center / Trypsin / α‐ヘリックス / P700 / 活性酸素 / トリプシン |
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| Research Abstract |
Structure and function of photosystem I (PSI) complexes from spinach thylakoid membranes have been studied.
1. Photoinhibitory illumination of PSI complexes caused an inactivation of the secondary electron acceptor, Al and the degradation of the reaction center proteins with no loss of the primary donor, P700.
2. To investigate the interaction between plastocyanin and PSI complex, chemical cross-linking technique with EDC,and immunostaining with anti-PSI-F-and antiplastocyain antisera were used for a probe of their accessibility. The data suggest the presence of two plastocyanin binding sites on PSI-F subunit.
3. Femtosecond transient absorption spectroscopy has been used to investigate the primary energy and electron transfer processes in PSI complexes from spinach, green algae and cyanobacterria.
4. PSI reaction center (RC) complex reconstituted into phosphatidylcholine liposomes was treated with trypsin and the polypeptide fragments, thus obtauned, were analyzed by amino acid sequencer. The results support the new folding model for PSI RC proteins proposed from X-ray crystallography.
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