| Project/Area Number |
07309006
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 総合 |
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| Research Field |
広領域
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
MORISHIMA Isao Kyoto University, Graduate School of Engineering, Professor, 工学研究科, 教授 (50026093)
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| Co-Investigator(Kenkyū-buntansha) |
MOGI Tateshi Tokyo University, Graduate School of Science, Research Associate, 理学部, 助手 (90219965)
HORI Hiroshi Osaka University, Faculty of Engineering Science, Research Associate, 基礎工学部, 助手 (20127294)
FUKUYAMA Keiichi Osaka University, Graduate School of Science, Professor, 理学部, 教授 (80032283)
HASE Toshiharu Osaka University, Protein Research Institute, Professor, 蛋白質研究所, 教授 (00127276)
KITAGAWA Teizo Institute of Molecular Science, Professor, 教授 (40029955)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥11,300,000 (Direct Cost: ¥11,300,000)
Fiscal Year 1996: ¥5,300,000 (Direct Cost: ¥5,300,000)
Fiscal Year 1995: ¥6,000,000 (Direct Cost: ¥6,000,000)
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| Keywords | Peroxidase / Ferredoxin / Nitrite Reductase / Oxgen Snsor Fix L / Cytochrome c Oxidase / Cytochrome P450 / 酸素センサーFixL / チトクロム酸化酵素 |
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| Research Abstract |
The Primary results in this research project are as follows :
1)The extensive mutation in horseradish peroxidase has revealed that the highly conserved hydrogen network in the distal site plays a key role in catalytic activity in peroxidases. The detailed molecular mechanism in peroxidase reaction was discussed.
2)The crystal structure of ARP,which shows specific high reactivity for luminol, was resolved and the substrate binding site was proposed. By using time-resolved resonance Raman spectroscopy, we examined the intermediate species in the reaction ARP and compared them with those of horseradish peroxidase.
3)We followed the reaction of cytochrome c oxidase with hydrogen peroxide and idetified some key inter mediates in the reaction.
4)The Regulation mechanism for the terminal oxidase in Escherichia coli was investigated by using the mutants.
5)The electron transfer in nitrite reductase, cytochrome cd_1, was examined by pulse radiolysis and reduction mechanism for the enzyme was proposed.
6)The systematic mutation in ferredoxin showed the specific interaction sites between ferredoxin and sulfite reductase.
7)We resolved crystal structure of another nitrite reductase, P450nor, and discussed the molecular mechanism for reduction of nitrite by the enzyme.
8)EPR was utilized for the investigation of the interaction between cytochrome P450cam and its electron donor, putidaredoxin. Some specific interactions were elucidated.
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