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Sterically Fixed Retinal‐Analogue Prevents Proton‐Pumping Activity in Bacteriorhodopsin
Author(s) -
Kölling Elisabeth,
Gärtner Wolfgang,
Oesterhelt Dieter,
Ernst Ludger
Publication year - 1984
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198400811
Subject(s) - bacteriorhodopsin , chromophore , steric effects , isomerization , chemistry , stereochemistry , halobacteriaceae , retinal , proton , photochemistry , biochemistry , membrane , physics , catalysis , halobacterium salinarum , quantum mechanics
The mode of action of bacteriorhodopsin has been studied using an all‐ trans and the 13‐ cis isomers of the retianl analogue 1 . Compound 1 is the first retianl analogue whose 13‐ cis isomer does not fit into the binding site of the apoprotein. Since the all‐ trans /13‐ cis isomerization in the protein cannot take place, the reconstituted chromophore with the all‐ trans isomer is not functionable.