Spectral Signatures of the Pentagonal Water Cluster in Bacteriorhodopsin
The exchange of protons between basic and acidic groups within proteins often involves transient protonation of amino acids and water molecules embedded in the protein matrix. One of the best studied proteins in this respect is Bacteriorohodopsin (BR), which works in the membrane of Halobacterium salinarium as a light-driven proton pump. The pumping process is triggered in the initial bR state by a photon absorption of an all-trans retinylidene chromophore, which is linked via a protonated Schiff base (pRSB) to the sidechain of Lys216. The subsequent photocycle comprises a series of intermediate states J, K, L, M, N and O, which are characterized by conformational and absorbance changes of the chromophore accompanying several elementary proton transfer processes. Upon completion of the photocycle one net proton has been transferred from the cyctoplasmic to the extracellular side against the proton gradient across the membrane. These proton exchange reactions can be monitored by time resolved infrared (IR) spectroscopy of the BR wild type and site specific mutants, which allow the localization of absorbance changes within the protein. Furthermore, these measurements have revealed the fundamental importance of internal water molecules in these processes as supported by recent large-scale QM/MM molecular dynamics studies of anharmonic IR spectra.
- Research Organization:
- Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- W-7405-ENG-48
- OSTI ID:
- 945894
- Report Number(s):
- LLNL-JRNL-405754; CPCHFT; TRN: US0901122
- Journal Information:
- ChemPhysChem, Vol. 9, Issue 18; ISSN 1439-4235
- Country of Publication:
- United States
- Language:
- English
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