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Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of proteorhodopsin

発表形態:
原著論文
主要業績:
単著・共著:
発表年月:
2018年09月
DOI:
10.1002/1873-3468.13219
会議属性:
査読:
リンク情報:

日本語フィールド

著者:
Fujisawa, Tomotsumi; Abe, Masahiro; Tamogami, Jun; Kikukawa, Takashi; Kamo, Naoki; Unno, Masashi
題名:
Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of proteorhodopsin
発表情報:
FEBS Letters 巻: 592 号: 18 ページ: 3054 - 3061
キーワード:
概要:
© 2018 Federation of European Biochemical Societies Proteorhodopsin (PR) is a microbial rhodopsin functioning as a light-driven proton pump in aquatic bacteria. We performed low-temperature Raman measurements of PR to obtain the structure of the primary photoproduct, the K intermediate (PRK). PRK showed the hydrogen-out-of-plane modes that are much less intense than those of bacteriorhodopsin as the prototypical light-driven proton pump from haloarchaea. The present results reveal the significantly relaxed chromophore structure in PRK, which can be coupled to the slow kinetics of the K intermediate. This structure suggests that PR transports protons using the small energy storage within the chromophore at the start of its photocycle.
抄録:

英語フィールド

Author:
Fujisawa, Tomotsumi; Abe, Masahiro; Tamogami, Jun; Kikukawa, Takashi; Kamo, Naoki; Unno, Masashi
Title:
Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of proteorhodopsin
Announcement information:
FEBS Letters Vol: 592 Issue: 18 Page: 3054 - 3061
An abstract:
© 2018 Federation of European Biochemical Societies Proteorhodopsin (PR) is a microbial rhodopsin functioning as a light-driven proton pump in aquatic bacteria. We performed low-temperature Raman measurements of PR to obtain the structure of the primary photoproduct, the K intermediate (PRK). PRK showed the hydrogen-out-of-plane modes that are much less intense than those of bacteriorhodopsin as the prototypical light-driven proton pump from haloarchaea. The present results reveal the significantly relaxed chromophore structure in PRK, which can be coupled to the slow kinetics of the K intermediate. This structure suggests that PR transports protons using the small energy storage within the chromophore at the start of its photocycle.


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