These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Similarity of bacteriorhodopsin structural changes triggered by chromophore removal and light-driven proton transport.
    Author: Ludlam GJ, Rothschild KJ.
    Journal: FEBS Lett; 1997 May 05; 407(3):285-8. PubMed ID: 9175869.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]