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High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle

Author

Listed:
  • Karl Edman

    (Uppsala University, Biomedical Centre)

  • Peter Nollert

    (Biozentrum, University of Basel
    UCSF)

  • Antoine Royant

    (Institut de Biologie Structurale, CEA-CNRS-Université Joseph Fourier
    European Synchrotron Radiation Facility)

  • Hassan Belrhali

    (European Synchrotron Radiation Facility)

  • Eva Pebay-Peyroula

    (Institut de Biologie Structurale, CEA-CNRS-Université Joseph Fourier)

  • Janos Hajdu

    (Uppsala University, Biomedical Centre)

  • Richard Neutze

    (Uppsala University, Biomedical Centre)

  • Ehud M. Landau

    (Biozentrum, University of Basel)

Abstract

Bacteriorhodopsin is the simplest known photon-driven proton pump1 and as such provides a model for the study of a basic function in bioenergetics. Its seven transmembrane helices2 encompass a proton translocation pathway containing the chromophore, a retinal molecule covalently bound to lysine 216 through a protonated Schiff base, and a series of proton donors and acceptors. Photoisomerization of the all-trans retinal to the 13-cis configuration initiates the vectorial translocation of a proton from the Schiff base, the primary proton donor, to the extracellular side, followed by reprotonation of the Schiff base from the cytoplasm. Here we describe the high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin, which is formed directly after photoexcitation. A key water molecule is dislocated, allowing the primary proton acceptor, Asp 85, to move. Movement of the main-chain Lys 216 locally disrupts the hydrogen-bonding network of helix G, facilitating structural changes later in the photocycle.

Suggested Citation

  • Karl Edman & Peter Nollert & Antoine Royant & Hassan Belrhali & Eva Pebay-Peyroula & Janos Hajdu & Richard Neutze & Ehud M. Landau, 1999. "High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle," Nature, Nature, vol. 401(6755), pages 822-826, October.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6755:d:10.1038_44623
    DOI: 10.1038/44623
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    Cited by:

    1. Alma P. Perrino & Atsushi Miyagi & Simon Scheuring, 2021. "Single molecule kinetics of bacteriorhodopsin by HS-AFM," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Partha Malakar & Samira Gholami & Mohammad Aarabi & Ivan Rivalta & Mordechai Sheves & Marco Garavelli & Sanford Ruhman, 2024. "Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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