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Published May 2, 1997 | public
Journal Article

Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer

Abstract

High resolution x-ray diffraction data from crystals of theRhodobacter sphaeroides photosynthetic reaction center (RC) have been collected at cryogenic temperature in the dark and under illumination, and the structures were refined at 2.2 and 2.6 angstrom resolution, respectively. In the charge-separated D+Q_AQ_B− state (where D is the primary electron donor (a bacteriochlorophyll dimer), and Q_A and Q_B are the primary and secondary quinone acceptors, respectively), Q_B− is located approximately 5 angstroms from the Q_B position in the charge-neutral (DQ_AQ_B) state, and has undergone a 180° propeller twist around the isoprene chain. A model based on the difference between the two structures is proposed to explain the observed kinetics of electron transfer from Q_A–Q_B to Q_AQ_B− and the relative binding affinities of the different ubiquinone species in the Q_B pocket. In addition, several water channels (putative proton pathways) leading from the Q_B pocket to the surface of the RC were delineated, one of which leads directly to the membrane surface.

Additional Information

© 1997 American Association for the Advancement of Science. Received 18 September 1996; accepted 10 March 1997. We thank M. Y. Okamura, M. L. Paddock, H. L. Axelrod, and M. S. Graige for insightful comments and discussions. This work was supported by grants from the National Institutes of Health (NIH GM13191, NIH GM45162). The rotation camera facility at SSRL is supported by the Department of Energy and by NIH. X-PLOR calculations were performed at the San Diego Supercomputer Center supported by NSF. The coordinates have been deposited in the Brookhaven Protein Data Bank with accession number 1aig and aij.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023