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首页> 外文期刊>The FEBS journal >Photoinduced formation of flavin radicals in BLUF domains lacking the central glutamine
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Photoinduced formation of flavin radicals in BLUF domains lacking the central glutamine

机译：缺乏中央谷氨酰胺的BLUF域中黄素自由基的光诱导形成

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摘要

Blue light receptors using FAD (BLUFs) facilitate blue light-induced signal transduction via light-induced rearrangement of hydrogen bonds between the flavin chromophore and a conserved glutamine side chain. Here, we investigated the photochemistry of the BLUF domain Slr1694 from Synechocystis sp. in which the glutamine side chain was removed. Without the glutamine, no red-shifted signaling state is formed, but light-induced proton-coupled electron transfer between protein and flavin takes place similarly as for the wild-type protein. However, the lifetime of the neutral flavin semiquinone-tyrosyl radical pair is greatly prolonged from 100ps to several nanoseconds, which indicates that the formation of radical intermediates drives the hydrogen bond rearrangement in BLUF photoactivation. Moreover, glutamine plays a central role in the molecular organization of the hydrogen bond network in the flavin-binding pocket, as its removal enhances electron transfer from tyrosine to the excited flavin, and enables competing electron transfer from a nearby tryptophan.
机译：使用FAD（BLUF）的蓝光受体通过黄素生色团与保守的谷氨酰胺侧链之间的氢键光诱导重排，促进了蓝光诱导的信号转导。在这里，我们研究了蓝藻属（Synechocystis sp。）BLUF结构域Srl1694的光化学。其中谷氨酰胺侧链被去除。没有谷氨酰胺，就不会形成红移的信号状态，但是光诱导的蛋白质与黄素之间的质子偶联电子转移与野生型蛋白质相似。但是，中性黄素半醌-酪氨酰基自由基对的寿命从<100ps大大延长到几纳秒，这表明自由基中间体的形成驱动BLUF光活化中的氢键重排。此外，谷氨酰胺在黄素结合口袋中氢键网络的分子组织中起着核心作用，因为谷氨酰胺的去除会增强电子从酪氨酸到受激发的黄素的转移，并使竞争的电子从附近的色氨酸竞争。

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