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  • 标题:Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center
  • 本地全文:下载
  • 作者:Richard H. G. Baxter ; Nina Ponomarenko ; Vukica Šrajer
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2004
  • 卷号:101
  • 期号:16
  • 页码:5982-5987
  • DOI:10.1073/pnas.0306840101
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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.
  • 关键词:bacterial photosynthesis ; secondary electron transfer ; Laue diffraction ; time-resolved crystallography ; quinones
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