Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of proteorhodopsin
Low-temperature Raman spectroscopy reveals small chromophore distortion in primary photointermediate of proteorhodopsin
复制标题
低温拉曼光谱揭示了原视紫红质初级光中间体中的微小发色团畸变
DOI:
10.1002/1873-3468.13219
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发表时间:
2018
期刊:
影响因子:
3.5
通讯作者:
Unno Masashi
中科院分区:
文献类型:
--
作者:
Fujisawa Tomotsumi;Abe Masahiro;Tamogami Jun;Kikukawa Takashi;Kamo Naoki;Unno Masashi
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). PRKshowed 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.