| Project/Area Number |
15K13660
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Inorganic chemistry
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
Matsuo Takashi 奈良先端科学技術大学院大学, 物質創成科学研究科, 准教授 (50432521)
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| Co-Investigator(Renkei-kenkyūsha) |
HIROTA Shun 奈良先端科学技術大学院大学, 物質創成科学研究科, 教授 (90283457)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | セレノシステイン / 金属酵素 / サブチリシン / 合成化学 / 酵素反応 / ヘテロ元素 / 触媒・化学プロセス |
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| Outline of Final Research Achievements |
A variety of artificial metallo-biocatalysts have been developed aiming at catalytic reactions based on reactivities of metal complexes in protein cores with highly-ordered structures. For molecular design of the catalysts, we pay attentions to characters of elements that coordinate to the centered metal ion. In this context, this project has focuses on the characters of selenium as a coordinating element although amino acids with a selenium atom have been rarely employed for the construction of artificial metalloenzymes. We have attempted to construct a metal coordination site with selenocystein in subtilisin, a protease readily obtainable from conventional vendors, through chemical modification and to incorporate several transition metal ions into the site. We successfully optimized the conditions for the incorporation of selenocysteine and found that the metalloenzyme is able to mediate the reduction of ketones in the presence of suitable reducing reagents.
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