Protein engineering studies on stable cytochrome c' aiming at enhancing NO binding
Project/Area Number |
16K07692
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Applied biochemistry
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Research Institution | Hiroshima University |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
河合 幸一郎 広島大学, 生物圏科学研究科, 教授 (30195028)
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Project Period (FY) |
2016-10-21 – 2019-03-31
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Project Status |
Completed (Fiscal Year 2018)
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Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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Keywords | NOセンサー / NO結合 / 蛋白質 / シトクロムc' / シトクロムc’ / シトクロムc' / ユスリカ / ヘモグロビン / ガス結合能 |
Outline of Final Research Achievements |
This study was aiming at enhancing NO binding ability of thermally stable cytochrome c', PHCP, using acidophilic midge haemoglobin as a model. Through this study, we succeeded in estimating NO binding affinity by measuring absorption spectral changes upon NO binding with PHCP, and in enhancing NO binding ability of PHCP by introducing mutations into PHCP. The resulting PHCP variants will be promising materials to be used as NO sensor proteins.
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Academic Significance and Societal Importance of the Research Achievements |
本研究は,代表者が専門とする蛋白質科学分野にユスリカの形態分類学を導入した点で,異分野を融合する学術的に独創的な試みであった。本研究の成果として得られた耐熱性を保持しNO結合能が向上した蛋白質(PHCP変異体)は,血管弛緩などの生理作用を示すNOを感度よく測定できるNOセンサー蛋白質として利用できる可能性があり,ひいてはNOをマーカーとして身体ストレスを簡便に検出できる意義がある。
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Report
(4 results)
Research Products
(27 results)
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[Journal Article] Stabilization of mesophilic Allochromatium vinosum cytochrome c′ through specific mutations modeled by a thermophilic homologue.2018
Author(s)
Yamane-Koshizawa, D., Fujii, S., Maruno, T., Kobayashi, Y., Yamanaka, M., Wakai, S., Sambongi, Y
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Journal Title
Biosci. Biotech. Biochem.
Volume: 82
Issue: 2
Pages: 304-311
DOI
Related Report
Peer Reviewed
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[Journal Article] Structural and functional insights into thermally stable cytochrome c' from a thermophile.2017
Author(s)
S. Fujii, H. Oki, K. Kawahara, D. Yamane, M. Yamanaka, T. Maruno, Y. Kobayashi, M. Masanari, S. Wakai, H. Nishihara, T. Ohkubo, Y. Sambongi.
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Journal Title
Protein Science
Volume: 26
Issue: 4
Pages: 737-748
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Pseudomonas aeruginosa cytochrome c551 denaturation by five systematic urea derivatives that differ in the alkyl chain length.2017
Author(s)
78.Kobayashi, S., Fujii, S., Koga, A., Wakai, S.,Matubayasi, N., Sambongi, Y
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Journal Title
Biosci. Biotech. Biochem.
Volume: 81
Issue: 7
Pages: 1274-1278
DOI
Related Report
Peer Reviewed
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[Journal Article] Comparative study on stabilization mechanism of monomeric cytochrome c5 from deep-sea piezophilic Shewanella violacea2016
Author(s)
.Masanari, M., Fujii, S., Kawahara, K., Oki, H., Tsujino, H., Maruno, T., Kobayashi, Y., Ohkubo, T., Wakai, S., Sambongi, Y
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Journal Title
Biosci. Biotech. Biochem.
Volume: 80
Issue: 12
Pages: 2365-2370
DOI
Related Report
Peer Reviewed
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