Title of article :
Internal water molecules of light-driven chloride pump proteins
Author/Authors :
Shibata، نويسنده , , Mikihiro and Muneda، نويسنده , , Norikazu and Ihara، نويسنده , , Kunio and Sasaki، نويسنده , , Takanori and Demura، نويسنده , , Makoto and Kandori، نويسنده , , Hideki، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2004
Pages :
4
From page :
330
To page :
333
Abstract :
Halorhodopsin and bacteriorhodopsin convert light into energy in archaea through light-driven chloride and proton pumps, respectively. Three water molecules are present in their active centers, which presumably stabilize the quadrupole structures and play crucial roles in pumps. The present low-temperature Fourier-transform infrared (FTIR) study revealed that hydration of the negative charges by the internal water molecules is much weaker in halorhodopsin than in bacteriorhodopsin, suggesting that chloride ion is stabilized by weak hydrogen bonds of waters in halorhodopsin.
Journal title :
Chemical Physics Letters
Serial Year :
2004
Journal title :
Chemical Physics Letters
Record number :
1785063
Link To Document :
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