Influence of the Chromophore Retinal and the State of Aggregation on the Proton/Hydroxyl Ion Flux Across Bacteriorhodopsin

  • Petra A. Burghaus
  • Norbert A. Dencher
Part of the NATO ASI Series book series (NSSA, volume 133)


The influence of the chromophore retinal in bacteriorhodopsin on the passive proton/hydroxide ion flux through the protein was examined. Bacteriorhodopsin was reconstituted into unilamellar lipid vesicles. Transmembrane pH-gradients were quickly established across the vesicular membrane and the induced kinetics of the fluorescence changes of the entrapped dye pyranine were compared for vesicles with incorporated native, chromophore-free, and regenerated protein. The H+/OH- diffusion across the apoprotein was considerably faster than through the protein containing covalently bound retinal. A linear dependence between the ΔpH decay time and the degree of regeneration was observed.


Purple Membrane Protein Moiety Vesicular Membrane Chromophore Retinal Halobacterium Halobium 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Petra A. Burghaus
    • 1
  • Norbert A. Dencher
    • 1
  1. 1.Biophysics Group, Department of PhysicsFreie Universität BerlinBerlin 33Germany

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