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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center
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Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center

机译：光合作用中心中光诱导结构变化的时间分辨晶体学研究

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摘要

Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochioris 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" Q(B) 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 Q(A) and Q(B).
机译：通过时间分辨晶体学实验研究了光在细菌反应中心的结构变化。用脉冲醌激光（630 nm，3 mJ / pulse，持续时间7 ns）在黑暗中和在3毫秒内，用泛醌重新溶解了绿芽孢杆菌（以前的红假单胞菌）的蛋白质晶体，并通过单色和Laue衍射进行了分析。 。单色数据的细化表明，泛醌仅在“近端” Q（B）结合位点结合。在明暗数据集之间未观察到明显的结构差异；特别是，没有检测到醌运动。通过假设延长的暗适应后“远侧”和“近侧”结合位点的平衡，该结果可能与先前的研究相吻合，其中泛醌的运动不是Q（A）和Q之间第一次电子转移的构象门（B）。

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