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(5‐demethyl)‐Bacteriorhodopsin analogue: its formation and light‐driven proton pump action
Author(s) -
Muradin-Szweykowska M.,
Amsterdam L.J.P.van,
Rodenburg L.J.M.,
Lugtenburg J.,
der Bend R.L.van,
Dam K.van
Publication year - 1983
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(83)80899-0
Subject(s) - bacteriorhodopsin , chromophore , proton , chemistry , retinal , ring (chemistry) , biophysics , retinaldehyde , photochemistry , stereochemistry , rhodopsin , biochemistry , membrane , organic chemistry , physics , biology , quantum mechanics
The binding of the isomers (all‐ trans , 13‐ cis , 11‐ cis and 9‐ cis ) of 5‐demethylretinal to bacterioopsin and the light—dark adaptation as well as the light‐driven proton pump action of the resulting bacteriorhodopsin analogue were studied. The (5‐demethyl)‐bacteriorhodopsinis formed ≈ 3‐times faster than unmodified bacteriorhodopsin and shows an efficient light‐driven proton pump action. These findings show that upon binding of retinal to bacterioopsin the protein forces the chromophore to adopt a more planar ring‐chain conformation than in free retinal.