Elucidation of membrane protein proton transfer dynamics by time-resolved vibrational spectroscopy
Project/Area Number |
23550022
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Physical chemistry
|
Research Institution | University of Hyogo |
Principal Investigator |
|
Project Period (FY) |
2011-04-28 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
|
Keywords | チトクローム酸化酵素 / 時間分解赤外分光法 / 共鳴ラマン分光法 / プロトンポンプ / 蛋白質ダイナミクス / 膜蛋白質 / 共役機構 / 蛋白質 / 新規赤外分光法 / 溶液内タンパク質 / 酸素還元反応 / 赤外分光 |
Outline of Final Research Achievements |
To investigate the coupling mechanism of the oxygen reduction reaction to water molecule and proton pumping in cytochrome c oxidase, new flow system that enable the time-resolved spectroscopy has been developed. By using this system, in the initial reaction process, heme a3 and His protein-reaction site interaction changed immediately changes to adjust the oxygen affinity. And it was also confirmed that it synchronizes with the open-close of the gate through water channel. This is the first example that observed the coupling mechanisms of the oxygen reduction reaction and the proton pumping in real time by the experimental observation. Furthermore, it was clarified that oxygen binds to CuB before ligate to heme a3, and it controlled the timing of the start of the oxygen reduction reaction. These observations exhibit that oxygen reduction reaction itself controlled the proton pumping mechanisms.
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Report
(5 results)
Research Products
(38 results)