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KINETIC AND SPECTROSCOPIC EFFECTS OF PROTEIN‐CHROMOPHORE ELECTROSTATIC INTERACTIONS IN BACTERIORHODOPSIN
Author(s) -
Warshel A.,
Ottoenghi M.
Publication year - 1979
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1979.tb07149.x
Subject(s) - bacteriorhodopsin , chromophore , chemistry , halobacteriaceae , photochemistry , absorption spectroscopy , electrostatics , kinetic energy , chemical physics , physics , biochemistry , halobacterium salinarum , optics , quantum mechanics , membrane
— Available pH effects on the absorption spectrum and on the rates of dark adaptation (all‐ trans → 13 ‐cis interconversion) of bacteriorhodopsin are analyzed in terms of a model based on protein‐chromophore electrostatic interactions. Plausible locations of three protein acid‐base groups controlling the spectrum and the activation energy of the thermal trans → 13‐ cis process are suggested. The importance of the protein charges in controlling the cycles of bacteriorhodopsin is indicated.