Time-resolved infrared spectroscopy of the thermophilic rhodopsin under various pressures and temperatures
| Project/Area Number |
15H06837
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Physical chemistry
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| Research Institution | Tohoku University (2016)
Institute for Molecular Science (2015) |
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Principal Investigator |
Kuroi Kunisato 東北大学, 大学院薬学研究科, 助教 (70757757)
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| Co-Investigator(Renkei-kenkyūsha) |
Tsukamoto Takashi 北海道大学, 大学院・先端生命科学研究院, 助教 (30744271)
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| Project Period (FY) |
2015-08-28 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 耐熱性ロドプシン / 時間分解赤外分光計測 / 高温 / 高圧 / 光反応 / 圧力 / 時間分解赤外分光法 / バクテリオロドプシン / 時間分解赤外計測 / 高圧条件 / 時間分解赤外分光 |
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| Outline of Final Research Achievements |
We investigated the photoreaction of the thermophilic rhodopsin (TR) by time-resolved Fourier transform infrared spectroscopy (TR-FTIR) under various temperature and pressure conditions to thermodynamically characterize its photoreaction. First, from the TR-FTIR measurement of TR and its mutants at 50 degree, we revealed the intramolecular proton transfer mechanism of TR. Second, from the TR-FTIR measurement of TR at various temperatures from 30 to 70 degrees, we found that the photoreaction mechanism of TR seemed to switch at about 40 degree. Finally, we developed the measurement system of high-pressure TR-FTIR, and applied it to the photoreaction of the bacteriorhodopsin (BR). We succeeded in measuring the TR-FTIR spectra of BR under high-pressure for the first time. However, due to the bad signal to noise ratio of the system, unfortunately we couldn’t apply that system to TR by the end of this project.
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Report
(3 results)
Research Products
(5 results)
