Literature DB >> 12512772

Internal water molecules of archaeal rhodopsins (Review).

Yuji Furutani1, Hideki Kandori.   

Abstract

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.

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Year:  2002        PMID: 12512772     DOI: 10.1080/0968768021000035069

Source DB:  PubMed          Journal:  Mol Membr Biol        ISSN: 0968-7688            Impact factor:   2.857


  3 in total

1.  Sensory rhodopsin-I as a bidirectional switch: opposite conformational changes from the same photoisomerization.

Authors:  Jun Sasaki; Hazuki Takahashi; Yuji Furutani; Hideki Kandori; John L Spudich
Journal:  Biophys J       Date:  2011-05-04       Impact factor: 4.033

2.  Protein-protein interaction changes in an archaeal light-signal transduction.

Authors:  Hideki Kandori; Yuki Sudo; Yuji Furutani
Journal:  J Biomed Biotechnol       Date:  2010-06-29

3.  The transporter-opsin-G protein-coupled receptor (TOG) superfamily.

Authors:  Daniel C Yee; Maksim A Shlykov; Ake Västermark; Vamsee S Reddy; Sumit Arora; Eric I Sun; Milton H Saier
Journal:  FEBS J       Date:  2013-09-23       Impact factor: 5.542

  3 in total

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