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Chromophore equilibria in bacteriorhodopsin.

U Fischer, D Oesterhelt

    Biophysical Journal
    |November 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    Bacteriorhodopsin (BR) chromophore dynamics reveal distinct intermediates and anion binding effects. Protonation state and anionic group interactions modulate the retinylidene Schiff base, explaining observed spectral shifts and equilibria.

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    Area of Science:

    • Biophysics
    • Photochemistry
    • Structural Biology

    Background:

    • Bacteriorhodopsin (BR) is a light-driven proton pump with complex chromophore equilibria.
    • Understanding BR's photochemical cycle and chromophore interconversions is crucial for its function.

    Purpose of the Study:

    • To investigate dark equilibria and kinetics of bacteriorhodopsin chromophores.
    • To elucidate the photochemical activity and structural basis of BR intermediates.

    Main Methods:

    • Spectroscopic analysis of bacteriorhodopsin chromophores.
    • Kinetic studies of chromophore interconversion.
    • Proton and anion binding experiments.

    Main Results:

    • Identified a millisecond-decaying 605-nm chromophore component, likely the O intermediate, formed by proton binding.

    Related Experiment Videos

  • Described an acidic purple complex (PCaL-) formation via anion binding (F- > Cl- > Br- > I- > ClO4-).
  • Characterized retinal isomer ratios in different states and a 500-nm chromophore formation via proton release.

    • Conclusions:

    • Proposed a model where retinylidene Schiff base protonation and anionic group interactions modulate the absorption spectrum.
    • Demonstrated pH-dependent stability changes of the purple complex at different temperatures.
    • Provided a comprehensive interpretation of BR chromophore behavior based on structural and electronic interactions.