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Published online on April 8, 2004, 10.1073/pnas.0306840101
PNAS | April 20, 2004 | vol. 101 | no. 16 | 5982-5987


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BIOPHYSICS
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center

Richard H. G. Baxter *, Nina Ponomarenko *, Vukica Srajer {dagger} {ddagger}, Reinhard Pahl {ddagger}, Keith Moffat {dagger} {ddagger} §, and James R. Norris * § ¶

*Department of Chemistry, University of Chicago, 5735 South Ellis Avenue, Chicago, IL 60637; {dagger}Department of Biochemistry and Molecular Biology and §Institute for Biophysical Dynamics, University of Chicago, 920 East 58th Street, Chicago, IL 60637; and {ddagger}Consortium for Advanced Radiation Sources, University of Chicago, 5640 South Ellis Avenue, Chicago, IL 60637

Edited by Robert Haselkorn, University of Chicago, Chicago, IL, and approved February 3, 2004 (received for review October 22, 2003)

Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" QB binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between QA and QB.

bacterial photosynthesis | secondary electron transfer | Laue diffraction | time-resolved crystallography | quinones

This paper was submitted directly (Track II) to the PNAS office.

Abbreviation: RC, reaction center.

Data deposition: The monochromatic model coordinates and structure factors have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 1R2C).

To whom correspondence should be addressed. E-mail: jrnorris{at}uchicago.edu.


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