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Sensitivity of the retinal circular dichroism of bacteriorhodopsin to the mutagenetic single substitution of amino acids: tyrosine
Author(s) -
El-Sayed M.A.,
Stern Lawrence J.,
Mogi Tatsushi,
Gobind Khorana H.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80178-l
Subject(s) - bacteriorhodopsin , circular dichroism , tyrosine , chemistry , substitution (logic) , amino acid substitution , sensitivity (control systems) , retinal , amino acid , stereochemistry , biochemistry , crystallography , biophysics , biology , mutation , membrane , electronic engineering , computer science , engineering , gene , programming language
Bacteriorhodopsin (bR) in the native purple membrane, in wild type expressed in E. coli and reconstituted in lipid vesicles, and its constituted mutants with substitutions of Tyr‐185 by Phe all are found to have different visible retinal CD spectra. The results strongly suggest that the environment of the retinal in bR determines the sign and heterogeneity of its visible retinal CD spectrum. This supports the recent proposal that the observed biphasic CD spectrum of bR is due to the superposition of the CD spectra having opposite signs of more than one type of bR rather than due to exciton coupling.