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Water‐mediated Spectral Shifts in Rhodopsin and Bathorhodopsin †
Author(s) -
Sekharan Sivakumar
Publication year - 2009
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.1751-1097.2008.00499.x
Subject(s) - rhodopsin , chromophore , counterion , absorbance , molecule , chemistry , hydrogen bond , photochemistry , chemical physics , crystallography , ion , organic chemistry , biochemistry , retinal , chromatography
The role of water molecules in spectral tuning of proteins has been left largely unexplored. This topic is important because changing hydrogen bond patterns during the activation process may lead to spectral shifts which can be of diagnostic value for the underlying structures. Arguments put forward in this article are based on spectral shift calculations of the rhodopsin and bathorhodopsin chromophore due to wat2a and 2b in the presence and absence of the counterion and of the amino acids lining the rhodopsin binding pocket. They show, among others, that a single water molecule can shift the absorbance by up to 0.1 eV or 34 nm depending on the environment of the chromophore.