Exploring the reaction mechanism of mitochondrial NADH-ubiquinone oxidoreductase (compelx I) using a specific inhibitor as a molecular probe
| Project/Area Number |
21880024
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Bioproduction chemistry/Bioorganic chemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
MURAI Masatoshi Kyoto University, 大学院・農学研究科, 助教 (80543925)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥2,756,000 (Direct Cost: ¥2,120,000、Indirect Cost: ¥636,000)
Fiscal Year 2010: ¥1,313,000 (Direct Cost: ¥1,010,000、Indirect Cost: ¥303,000)
Fiscal Year 2009: ¥1,443,000 (Direct Cost: ¥1,110,000、Indirect Cost: ¥333,000)
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| Keywords | ミトコンドリア / 複合体-I / キナゾリン / ユビキノン / 光親和性標識 / アセトゲニン / 生物有機化学 |
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| Research Abstract |
Mitochondrial NADH-ubiquinone oxidoreductase (complex I) catalyzes the initial reaction of respiratory chain, forming the electrochemical gradient for ATP synthesis. Using a photo-reactive quinazoline analogue, the head researcher revealed a new information about the interfacial region between hydrophilic and hydrophobic domains of complex I that is thought to be important for ubiqinone reduction and energy transduction.
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Report
(3 results)
Research Products
(37 results)
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[Journal Article] Characterization of the ubiquinone binding site in alterative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling2010
Author(s)
Murai, M., Yamashita, T., Senoh, M., Mashimo, Y., Kataoka, M., Kosaka, H., Matsuno-Yagi, A., Yagi, T., Miyoshi, H.
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Journal Title
Biochemistry 49
Pages: 2973-2980
Related Report
Peer Reviewed
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[Journal Article] Characterization of the ubiquinone binding site in alternative NADH-ubiquinone oxidoreductase of Saccharomyces cerevisiae py photoaffinity labeling2010
Author(s)
Murai, M., Yamashita, T., Senoh, M., Mashimo, Y., Kataoka, M., Kosaka, H., Matsuno-Yagi, A., Miyoshi, H.
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Journal Title
Biochemistry 49
Pages: 2973-2980
Related Report
Peer Reviewed
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