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Bacteriorhodopsin: lipid environment and conformational changes.

E P Bakker, M Eisenbach, H Garty

    Progress in Clinical and Biological Research
    |January 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

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    Altering purple membrane lipids slows bacteriorhodopsin

    Area of Science:

    • Biochemistry
    • Biophysics
    • Membrane Biology

    Background:

    • Purple membrane contains bacteriorhodopsin, a light-driven proton pump.
    • Protein-protein interactions in the membrane influence its function.

    Purpose of the Study:

    • To investigate the role of lipids in bacteriorhodopsin's proton transfer mechanism.
    • To explore light-induced conformational changes in bacteriorhodopsin.

    Main Methods:

    • Lipid exchange in purple membrane complexes.
    • Spectroscopic analysis of the bacteriorhodopsin photocycle.
    • Proton release and accumulation measurements at varying pH.

    Main Results:

    • Modified complexes showed a 10-20 fold slower photocycle.

    Related Experiment Videos

  • The ratio of proton release to M412 accumulation varied with pH (0.4-1.5).
  • Evidence for light-induced conformational changes affecting proton binding/release.

    • Conclusions:

    • Lipid environment significantly impacts bacteriorhodopsin's proton pumping efficiency.
    • Conformational changes in the protein's nonchromophore regions are light-induced.
    • Proton transfer involves simultaneous binding and dissociation on different membrane sides.