| Project/Area Number |
18550149
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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 |
Chemistry related to living body
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| Research Institution | Nagoya University (2007)
Tokyo Institute of Technology (2006) |
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Principal Investigator |
KAMACHI Toshiaki Nagoya University, Department of Engineering, Associate Professor (30272694)
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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 |
¥4,120,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | EQCM / Cytochrome Ca / ヒドロゲナーゼ / シトクロムC_3 / シトクロム |
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| Research Abstract |
Cytochrome c3 from Desulfovibrio vulgaris has four hemes per molecule, and a redox change at the hemes alters the conformation of the protein, leading to a redox-dependent change in the interaction of cytochrome c3 with redox partners (an electron acceptor or an electron donor) .The redox-dependent change in this interaction was directly monitored by the high-performance electrochemical quartz crystal microbalance (EQCM) technique that has been improved to give high sensitivity in solution. In this method, cytochrome c3 molecules in solution associate electrostatically with a viologen-immobilized quartz crystal electrode as a monolayer, and redox of the associating cytochrome c3 is controlled by the immobilized viologen. This technique makes it possible to measure the access of cytochrome c3 to the electrode or repulsion from the electrode, and hence interconversion between an electrostatic complex and an electron transfer complex on the cytochrome c3 and the viologen as a mass change accompanying a potential sweep is monitored. In addition, simultaneous measurement of a niece change and a potential step reveals that the cytochrome c3 stores electrons when the four hemes are reduced (an electron pool effect), that is, the oxidized cytochrome c3 facilitates acceptance of electrons from the immobilized viologen molecule, but the reduced cytochrome c3 donates the accepted electrons to the viologen with difficulty.
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