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

Karl Edman, Peter Nollert, Antoine Royant, Hassan Belrhali, Eva Pebay-Peyroula (), Janos Hajdu, Richard Neutze () and Ehud M. Landau ()
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Karl Edman: Uppsala University, Biomedical Centre
Peter Nollert: Biozentrum, University of Basel
Antoine Royant: Institut de Biologie Structurale, CEA-CNRS-Université Joseph Fourier
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

Nature, 1999, vol. 401, issue 6755, 822-826

Abstract: 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.

Date: 1999
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DOI: 10.1038/44623

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