Correlation between dynamic structure and catalytic function of flavoenzymes
| Project/Area Number |
62570110
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Tokushima University |
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Principal Investigator |
AKI Kenji Institute for Enzyme Research, Professor, 酵素制御学部門, 教授 (20035405)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUSHIMA Akemi Institute for Enzyme Research, Technical assistant, 酵素制御学部門, 教務員 (70116862)
MAEDA Kazuko Institute for Enzyme Research, Research assistant, 酵素制御学部門, 助手 (60116879)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1988: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1987: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | flavoenzyme / domain / oxidation-reduction / limited proteolysis / fluorescence depolarization and lifetime / circular dichroism / 電子スピン共鳴 / 電子伝達 / フラビン / セミキノン / 螢光特性 / 酵素活性 / フラビン セミキノン / 蛍光偏光解消 |
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| Research Abstract |
Flavoenzymes, lipoate dehydrogenase and flavocytochrome B_2 was studied on correlation between the dynamic structure and catalytic function. The protein structures were determined by circular dichroism and fluorescence. The catalytic functions were measured by enzyme kinetics and electron spin resonace.
Lipoate dehydrogenase was composed of four domains. NAD-binding domain fluctuated to elevate efficiency of electron transfer. Flavocytochrome B_2 was composed of two domains, flavin-binding domain which had a diaphorase activity and heme-binding domain. complex formation of both domains suppressed a diaphorase activity and induced a lactate dehydrogenase activity.
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Report
(3 results)
Research Products
(8 results)
