| Project/Area Number |
24655153
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Chemistry related to living body
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| Research Institution | Osaka University |
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Principal Investigator |
FUJIEDA Nobutaka 大阪大学, 工学(系)研究科(研究院), 助教 (00452318)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 非ヘム鉄酵素 / 酸化的自己修飾 / 翻訳後化学修飾 / ビルトイン補酵素 / 人工金属酵素 / 金属タンパク質 / 翻訳後修飾 / 非天然アミノ酸 / 自己水酸化反応 |
|---|
| Research Abstract |
Recently, many self-hydroxylation reactions have reported, which occurred of aromatic amino acids lying close to mononuclear and dinuclear iron and copper binding site. In this study, we utilized cupin family protein bearing three or four histidine binding motif (3-His or 4-His motif) as metal binding scaffold. In the mutant introduced one tyrosine into the location of Ile49 or Trp56, non-natural occurring unusual spectral species around 800 nm have been found. Thus, the modification method presented in this study is very powerful to construct new functional protein for novel devices of bioelectronics and artificial metalloenzyme to be able to catalyze multielectron transfer reactions.
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