Probing the intercellular traffic mechanism of ubiquinone using synthetic molecular probes
Project/Area Number |
23780116
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Bioproduction chemistry/Bioorganic chemistry
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Research Institution | Kyoto University |
Principal Investigator |
MURAI Masatoshi 京都大学, 大学院・農学研究科, 助教 (80543925)
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Co-Investigator(Renkei-kenkyūsha) |
MIYOSHI Hideto 京都大学, 大学院・農学研究科, 教授 (20190829)
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Project Period (FY) |
2011 – 2012
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Project Status |
Completed (Fiscal Year 2012)
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Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | ユビキノン / ミトコンドリア / 光親和性標識 / Click Chemistry / 複合体-I / 出芽酵母 |
Research Abstract |
Ubiquinone (UQ) is an essential electron carrier of the mitochondrial respiratory system. However, resent studies suggest the existence of the mitochondrial proteins, which use UQ as an important cofactor. We revealed mitochondrial ubiquinone-binding protein Coq10 accommodates UQ using synthetic UQ-probes.We also carried out photoaffinity labeling studies of mitochondrial NADH-ubiquinone oxidoreductase (complex I) using photolabile complex I inhibitors. We revealed that inhibitor/quinone-binding pocket formed at the interface of the PSST, 49 kDa, and ND1 subunits. These results strongly support our idea that this region exclusively accommodates chemically diverse complex I inhibitors in a manner dependent on their structural properties
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Report
(3 results)
Research Products
(43 results)
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[Journal Article] Localization of ubiquinone-8 in the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae2011
Author(s)
Casutt,M. S., Nedielkov,R., Wendelspiess, S., Vossler,S., Gerken,U., Murai, M., Miyoshi,H., Moller,H. M. andSteuber,J
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Journal Title
J. Biol. Chem
Volume: 286
Pages: 40075-40082
Related Report
Peer Reviewed
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[Journal Article] Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae: evidence for a ternary complex mechanism2011
Author(s)
Yang,Y., Yamashita,T., Nakamaru-Ogiso,E., Hashimoto,T., Murai, M., Igarashi,J., Miyoshi, H., Mori,N., Matsuno-Yagi,A., Yagi,T. andKosaka,H
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Journal Title
J. Biol. Chem
Volume: 286
Pages: 9287-9297
Related Report
Peer Reviewed
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[Journal Article] Synthesis and characterization of photoaffinity probe of acetogenin, a strong inhibitor of mitochondrial complex I2011
Author(s)
Yamamoto, S., Abe, M., Nakanishi, S., Murai, M., and Miyoshi, H.
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Journal Title
Tetrahedron Lett
Volume: 52
Issue: 24
Pages: 3090-3093
DOI
Related Report
Peer Reviewed
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[Journal Article] Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae: evidence for a ternary complex mechanism2011
Author(s)
Yang Y, Yamashita T, Nakamaru-Ogiso E, Hashimoto T, Murai M, Igarashi J, Miyoshi H, Mori N, Matsuno-Yagi A, Yagi T, Kosaka H
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Journal Title
The Journal of Biological Chemistry
Volume: 286
Pages: 9287-9297
Related Report
Peer Reviewed
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