Abstract
In bright light the photosynthetic reaction center (RC) of Rhodobacter sphaeroides stabilizes the P+870·Q−A charge-separated state and thereby minimizes the potentially harmful effects of light saturation. Using X-ray diffraction we report a conformational change that occurs within the cytoplasmic domain of this RC in response to prolonged illumination with bright light. Our observations suggest a novel structural mechanism for the regulation of electron transfer reactions in photosynthesis.
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Acknowledgements
We thank staff of the European Synchrotron Radiation Facility, the Swiss Light Source and MaxLab for experimental support. We acknowledge support from the Swedish Strategic Research Foundation (SSF), SWEGENE, Swedish Research Council (VR) and the European Commission Improving Human Potential program.
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Supplementary information
Supplementary Fig. 1
Proteins and cofactors participating in electron movements within the photosynthetic membrane. (PDF 70 kb)
Supplementary Fig. 2
Absorption spectra recorded from a single RC crystal. (PDF 96 kb)
Supplementary Fig. 3
Long distance overview of the light-driven electron density changes within the RC. (PDF 182 kb)
Supplementary Fig. 4
The refined structural model and σA-weighted 2Fobs − Fcalc electron density map illustrated within the mobile region of the H-subunit. (PDF 250 kb)
Supplementary Table 1
Crystallographic data and refinement statistics. (PDF 49 kb)
Supplementary Table 2
Statistical analysis of reproducible difference density peaks. (PDF 17 kb)
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Katona, G., Snijder, A., Gourdon, P. et al. Conformational regulation of charge recombination reactions in a photosynthetic bacterial reaction center. Nat Struct Mol Biol 12, 630–631 (2005). https://doi.org/10.1038/nsmb948
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DOI: https://doi.org/10.1038/nsmb948
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