Pulsed EPR analysis of the photo-induced triplet radical pair in the BLUF protein SyPixD : Determination of the protein-protein distance and orientation in the oligomeric protein
Pulsed EPR analysis of the photo-induced triplet radical pair in the BLUF protein SyPixD : Determination of the protein-protein distance and orientation in the oligomeric protein
复制标题
BLUF 蛋白 SyPixD 中光诱导三重态自由基对的脉冲 EPR 分析：测定寡聚蛋白中的蛋白-蛋白距离和方向
DOI：
10.1007/s00723-011-0237-1
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发表时间：
2011
影响因子：
1
通讯作者：
Shinji Masuda and Hiroyuki Mino
中科院分区：
文献类型：
--
作者：
Toru Kondo;Shinji Masuda and Hiroyuki Mino
通过脉冲电子顺磁共振（EPR）光谱研究了BLUF蛋白SyPixD中的光诱导自由基对FADH·和Y8·以及。蓝光在 150 K 下照射 30 分钟，然后在照射期间冷却至 50 K，诱导稳定的自由基对。 EPR 信号的特征是具有完整 S= 1 自旋态的 Pake 双峰信号。该自由基对用作探针来分析 SyPixD 的寡聚物。通过脉冲电子-电子双共振 (PELDOR) 和方向选择研究了复合物中 PixD 蛋白的相对排列。基于晶体中的十聚体结构，讨论了 PELDOR 结果的可能结构。
A photo-induced radical pair of FADH·and Y8·and in BLUF protein SyPixD was studied by pulsed electron paramagnetic resonance (EPR) spectroscopy. Blue light illumination at 150 K for 30 min followed by cooling to 50 K during illumination induced the stable radical pair. The EPR signal has been characterized by a Pake doublet signal with completeS= 1 spin state. The radical pair was utilized as a probe to analyze the oligomer of SyPixD. The relative arrangement of PixD proteins in the complex was investigated by pulsed electron–electron double resonance (PELDOR) with the orientation selection. Based on the decameric structure in the crystal, the possible structure for the PELDOR results was discussed.