| Project/Area Number |
13558069
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
環境保全
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| Research Institution | Tohoku University |
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Principal Investigator |
SHIMIZU Toru Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Research Associate, 多元物質科学研究所, 教授 (40118956)
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| Co-Investigator(Kenkyū-buntansha) |
KUROKAWA Hirofumi Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Research Associate, 多元物質科学研究所, 助手 (80359546)
IGARASHI Jotaro Tohoku University, Institute of Multidisciplinary Research for Advanced Materials, Research Associate, 多元物質科学研究所, 助手 (80375162)
佐上 郁子 東北大学, 多元物質科学研究所, 講師 (10143033)
松井 敏高 東北大学, 多元物質科学研究所, 助手 (90323120)
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| Project Period (FY) |
2001 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥12,700,000 (Direct Cost: ¥12,700,000)
Fiscal Year 2004: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2003: ¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2002: ¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2001: ¥3,500,000 (Direct Cost: ¥3,500,000)
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| Keywords | Molecular switch / Sensor enzyme / Heme sensor / cAMP / Protein microarray / Protein-protein interaction / redox states / Signal transduction / 蛋白-蛋白相互作用 / シグナル / シトクロムP450 / 一酸化窒素 / 環境ホルモン / 電子移動 / キメラ / 遺伝子工学 / 薬物代謝 / チトクロムP450 |
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| Research Abstract |
Cytochrome P450s activate carcinogenetic activities and toxicities of various environmental chemicals including benzpyrene, aflatoxin, haloethanes. However, cytochrome P450s are also involved in metabolism and degradation of various environmental chemicals. Therefore, it is possible that we can construct efficient and useful environmental bioremediation enzymes if the degradation properties of cytochrome P450s can be used. A physiologically important gas, nitric oxide (NO), is synthesized by nitric oxide synthase whose active site structure is the sameas those of cytochrome P450s. On the other hand, there are many sensor enzymes and sensor proteins, where electron introduction, light illumination, bindings of calcium ion, CO, NO, molecule oxygen and various carcinogens induced certain protein conformational changes. The changes became signals that transmit to catalytic domain and switch the catalysis on/off. In the present study, we examined electron transfer process and protein-protein interactions of a calcium sensor protein, neuronal NO synthase. Then, we constructed chimeric enzymes composed of the calcium sensor domain of NO synthase and the have-bound active site of cytochrome P450. We examined efficiencies of electron transfer and catalysis of the generated calcium sensor chimeric enzymes with the an of a novel molecular switching enzyme. It was found that the chimeric enzyme functions as a calcium sensor enzyme. Furthermore, we examined structure and function relationships of a new redox sensor enzyme, Ec DOS. It was found that Ec DOS is also CO and NO sensor enzyme, because the catalysis was strongly inhibited by CO and NO. As the last step of this project study, we characterized potential heme-sensor enzyme, SOUL. In summary, the study provided the possibility to construct novel sensor enzymes with efficient biodegradation properties of environmental chemicals.
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