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首页> 外文期刊>Biochemistry >Spectroscopic Studies of the AppA BLUF Domain from Rhodobacter sphaeroides: Addressing Movement of Tryptophan 104 in the Signaling State
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Spectroscopic Studies of the AppA BLUF Domain from Rhodobacter sphaeroides: Addressing Movement of Tryptophan 104 in the Signaling State

机译：球形球形红细菌AppA BLUF结构域的光谱研究：处理色氨酸104在信号状态下的运动

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摘要

Previous crystallographic studies of the AppA BLUF domain indicated that Trp104 is capable of undertaking alternate conformations depending on the length of the BLUF domain. A BLUF domain containing a C-terminal deletion (AppA1−126) reveals that Trp104 is partially solvent exposed while a BLUF domain containing a slightly longer carboxyl terminal region (AppA17−133) shows that Trp104 is deeply buried. This observation has led to a model proposing that Trp104 moves from a deeply buried position in the dark state to a solvent-exposed position in the light excited state. In this study we investigated whether there is indeed movement of Trp104 upon light excitation using a combination of NMR and absorption spectroscopy, steady-state fluorescence, and acrylamide quenching of tryptophan fluorescence. Our results indicate that AppA17−133 and AppA1−126 contain Trp104 in distinct alternate conformations in solution and that light absorption by the flavin causes partial movement/uncovering of Trp104. However, we conclude that light exposure does not cause dramatic change of Trp104 from “Trp-in” to “Trp-out” conformations (or vice versa) upon light absorption. These results do not support a model of Trp104 movement as a key output signal
机译：AppA BLUF结构域的先前晶体学研究表明，根据BLUF结构域的长度，Trp104能够进行其他构象。包含C末端缺失的BLUF域（AppA1-126）揭示Trp104部分暴露于溶剂中，而包含稍长的羧基末端区域（AppA17-133）的BLUF域表明Trp104被深埋。该观察结果导致提出了一个模型，该模型提出了Trp104从暗状态下的深埋位置移动到光激发状态下的溶剂暴露位置。在这项研究中，我们使用NMR和吸收光谱，稳态荧光和色氨酸荧光的丙烯酰胺猝灭相结合，研究了光激发时Trp104是否确实存在。我们的结果表明，AppA17-133和AppA1-126在溶液中包含明显不同的交替构型的Trp104，黄素的光吸收会导致Trp104的部分移动/发现。但是，我们得出的结论是，在光吸收时，曝光不会引起Trp104从“ Trp-in”构型到“ Trp-out”构型的剧烈变化（反之亦然）。这些结果不支持Trp104运动模型作为关键输出信号

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