Abstract:
: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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Bergo VB,Spudich EN,Spudich JL,Rothschild KJdoi
10.1021/bi802180asubject
Has Abstractpub_date
2009-02-10 00:00:00pages
811-3issue
5eissn
0006-2960issn
1520-4995pii
10.1021/bi802180ajournal_volume
48pub_type
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