2014 Fiscal Year Final Research Report
The structural insight into ROS suppression mechanism of type II NADH dehydrogenase (NDH-2)
Project/Area Number |
25840036
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Functional biochemistry
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Research Institution | Kagawa University |
Principal Investigator |
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Project Period (FY) |
2013-04-01 – 2015-03-31
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Keywords | 活性酸素 / 反応機構 / フラボプロテイン / 基質結合部位 / NADH脱水素酵素 / ミトコンドリア / 電子伝達系 |
Outline of Final Research Achievements |
To elucidate the radical oxygen-suppression mechanism of mitochondrial type-II NADH dehydrogenase (NDH-2), we investigated biochemical properties of NDH-2 and its Thr239 mutant which have relatively high non-physiological NADH oxidase activity compared with wild type enzyme. By the kinetics, spectrographic and physicochemical analysis, it was strongly suggested that the formation of the charge-transfer complex between FAD-semiquinone, which is generated in the enzyme reaction process, and substrate NADH is responsible for the suppression of radical oxygen.
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Free Research Field |
生化学 生理学
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