| Project/Area Number |
24350086
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | University of Hyogo |
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Principal Investigator |
KITAGAWA Teizo 兵庫県立大学, 生命理学研究科, 名誉教授 (40029955)
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| Co-Investigator(Kenkyū-buntansha) |
OGURA Takashi 兵庫県立大学, 生命理学研究科, 教授 (70183770)
NAGATOMO Shigenori 筑波大学, 数理物質科学研究科, 講師 (80373190)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2014: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2013: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2012: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
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| Keywords | 生物物理 / 蛋白質 / シグナル伝達 / 生体分子 / 分子認識 / 振動分光 / 共鳴ラマン散乱 |
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| Outline of Final Research Achievements |
Cavity mutant human Hb, which lacks the Fe-His bond in either the α or β subunit but can bind four O2 molecules, was prepared. Its oxygen binding curve was determined, and higher order structural changes upon O2 binding were investigated with 1H NMR, V- and UV-resonance Raman, and nearUV CD spectra. Spectroscopic measurements revealed that the quaternary structure change did not occur upon ligand binding. The absence of Fe-His bond in α froze Hb in T while that of β raised the affinity of α. Resonance Raman spectra of NO sensor protein, mammalian sGC and its model protein, bacterial H-NOX, were investigated.
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