Internal water molecules of archaeal rhodopsins (Review)

被引：24

作者：

Furutani, Y ^{[1
]}

Kandori, H ^{[1
]}

机构：

[1] Nagoya Inst Technol, Dept Appl Chem, Showa Ku, Nagoya, Aichi 4668555, Japan

来源：

MOLECULAR MEMBRANE BIOLOGY | 2002年 / 19卷 / 04期

关键词：

proton pump; signal transduction; hydrogen-bonding network; low-temperature FTIR spectroscopy; O-H stretching vibration;

D O I：

10.1080/0968768021000035069

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Archaeal rhodopsins possess retinal molecule as their chromophores, and their light-energy and light-signal conversions are triggered by all-trans to 13-cis isomerization of the retinal chromophore. Relaxation through structural changes of protein then leads to functional processes, light-driven ion pump or transducer activation. Internal water molecules were considered to play an important role in the functional processes of archaeal rhodopsins, although limited information has been obtained about the structure and function of internal water molecules. Recent progress in Fourier-transform infrared (FTIR) spectroscopy and X-ray crystallography provided new information of water molecules inside archaeal rhodopsins, This article reviews studies on internal water molecules of archaeal rhodopsins by means of low-temperature FTIR spectroscopy.

引用

页码：257 / 265

页数：9

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