| Project/Area Number |
18570045
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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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・分子
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| Research Institution | Tokyo Metropolitan University |
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Principal Investigator |
NAGASHIMA Kenji Tokyo Metropolitan University, Dept., Biological Science, Assistant Prof (80264589)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,860,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥360,000)
Fiscal Year 2007: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2006: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Photosynthesis / Electron transfer / Cvtochrome / Electron donor / Heme / Redox potential / Reaction center / Photosynthetic bacteria / 遺伝子操作 / 光化学反応中心 / 進化 |
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| Research Abstract |
1.New electron carrier proteins working as electron donors to the reaction center complex have been searched in purple photosynthetic bacteria.
(1)New membrane-bound cytochrome c with a molecular mass of 50 kDa was found in a marine species, Rhodovulum sulfidophilum. Growth tests using mutants lacking this cytochrome showed that this cytochrome can completely support photosynthetic cyclic electron transport, as well as a popular electron carrier, cytochrome c_2. This new cytochrome was named cytochrome c_2m, taking into account its high sequence similarity with the cytochrome c_2 at the core region.
(2)A c-type cytochrome with a molecular mass of 25 kDa was newly found as a potential electron donor to the reaction center in aβ-purple bacterium, Rubrivivax gelatinosus. Based on sequence analyses, this cytochrome was identified as a homolog of cytochrome c4, which physiological functions have not been well clarified. In R gelatinosus, growth tests for the mutants lacking this cytochrome showed that this cytochrome can contribute to the photosynthetic electron transfer. This is the first experimental evidence to show that cytochrome c_4 can work as a physiological electron donor to the reaction center.
2.Redox midpoint potentials of two low-potential hemes in the tetrahemic cytochrome subunit bound to the reaction center have been raised about 60 mV by site-directed mutagenesis. These alterations resulted in changes in the rates of electron transfer from the high-potential hemes to the special pair of bacteriochlorophylls when peripheral redox potentials were lowered below the new midpoint potentials of the low-potential hemes. It was suspected that midpoint potentials of hemes are dynamically changed, depending on the redox states of the neighboring hemes.
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