Extreme Functionalization of Hemoproteins upon the Direct Chemical Modification to Heme Framework
| Project/Area Number |
14380291
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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 | 一般 |
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| Research Field |
Bioorganic chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
HAYASHI Takashi Kyushu University, Faculty of Engineering, Associate Professor, 大学院・工学研究院, 助教授 (20222226)
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| Co-Investigator(Kenkyū-buntansha) |
HISAEDA Yoshio Kyushu University, Faculty of Engineering, Professor, 大学院・工学研究院, 教授 (70150498)
島田 秀夫 慶應義塾大学, 医学部, 助教授 (80095611)
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| Project Period (FY) |
2002 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥14,400,000 (Direct Cost: ¥14,400,000)
Fiscal Year 2004: ¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2003: ¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2002: ¥6,800,000 (Direct Cost: ¥6,800,000)
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| Keywords | myoglobin / reconstitution / artificial heme / iron porphyicene / dioxygen affinit / peroxidase / carbon monoxide affinity / prosthetic group / ヘムタンパク質 / ペルオキシダーゼ活性 / 鉄コロール / タンパク質機能変換 / ペルキオシダーゼ / ペプオキシゲナーゼ / タンパク質再構成 / 過酸化水素 / グアイアコール / 中間体 / タンパク質機能化 / 酸素錯体 / 酸素センサー / 自動酸化 |
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| Research Abstract |
The incorporation of an artificially created heme into an apohemoprotein is a unique method for introducing a new chemical function into a protein. In this project, we mainly focused on a modification of heme framework to improve the function and/or create a new function in myoglobin. The summary of our recent results are shown as follows:
1.An iron porphycene as a structural isomer of the heme was inserted into apomyoglobin. The obtained reconstituted myoglobin showed an extremely high dioxygen affinity.
2.The reconstituted myoglobin with the iron porphycene showed peroxidase/peroxygenase activity. In addition, the compound III formation in the presence of hydrogen peroxide was firstly observed in myoglobin. Furthermore, a hybrid myoglobin which was prepared by heme-propionate modification and amino-acid mutation showed high peroxidase activity and is a good catalyst toward bisphenol A degradation.
3.Unusual dioxygen selectivity was obtained by introducing a hydrophobic cluster at the terminal two heme-propionate side chains.
These results suggest that the replacement of native heme with an artificially created prosthetic group will serve as a new way to create a functionalized hemoprotein.
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Report
(4 results)
Research Products
(30 results)
