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Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light‐driven proton transport
Author(s) -
Ludlam Gary J.,
Rothschild Kenneth J.
Publication year - 1997
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/s0014-5793(97)00351-7
Subject(s) - bacteriorhodopsin , rhodopsin , chromophore , chemistry , protonation , proton transport , halobacterium , halobacteriaceae , proton , biophysics , proton pump , conformational change , photoprotein , crystallography , membrane , photochemistry , stereochemistry , halobacterium salinarum , biochemistry , retinal , biology , atpase , ion , physics , organic chemistry , quantum mechanics , bioluminescence , enzyme
Bacteriorhodopsin (bR) is the light‐driven proton pump found in the purple membrane of Halobacterium salinarium . A series of conformational changes occur during the bR photocycle which involve alterations in buried‐helical structure as well as in the protonation state of Asp residues which are part of the proton transport pathway. Here we report evidence that similar conformational changes occur upon removal of the retinylidene chromophore of bacteriorhodopsin to form the apoprotein bacterioopsin (bO). This suggests a simple ligand‐binding model of proton transport in bacteriorhodopsin which may have relevance to other transport and signal transducing membrane proteins including the visual photoreceptor rhodopsin.