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Biochemistry. 2009 Feb 10;48(5):811-3. doi: 10.1021/bi802180a.

Active water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay.

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  • 1Department of Physics, Molecular Biophysics Laboratory, and Center for Photonics, Boston University, Boston, Massachusetts 02215, USA.


We detect internal water molecules in a membrane-embedded receptor-transducer complex and demonstrate water structure changes during formation of the signaling state. Time-resolved FTIR spectroscopy reveals stimulus-induced repositioning of one or more structurally active water molecules to a significantly more hydrophobic environment in the signaling state of the sensory rhodopsin II (SRII)-transducer (HtrII) complex. These waters, distinct from bound water molecules within the SRII receptor, appear to be in the middle of the transmembrane interface region near the Tyr199(SRII)-Asn74(HtrII) hydrogen bond. We conclude that water potentially plays an important role in the SRII --> HtrII signal transfer mechanism in the membrane's hydrophobic core.

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