Structural Change of a Cofactor Binding Site of Flavoprotein Detected by Single-Protein Fluorescence Spectroscopy at 1.5 K
Structural Change of a Cofactor Binding Site of Flavoprotein Detected by Single-Protein Fluorescence Spectroscopy at 1.5 K
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DOI：
10.1103/physrevlett.106.078101
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发表时间：
2011-02-15
影响因子：
8.6
通讯作者：
Watanabe, Masakatsu
中科院分区：
文献类型：
--
作者：
Fujiyoshi, Satoru;Hirano, Mitsuharu;Watanabe, Masakatsu
用单光子激发法测量了单个黄素蛋白在1.5K温度下的可见荧光光谱。研究的黄素蛋白是一种光开关酶，光活化腺苷酸环化酶。光谱的时间过程显示，在黄素辅因子结合位点的氢键周围以10（-3）s（-1）的速率发生结构变化。
The visible fluorescence spectrum of single flavoprotein at a temperature of 1.5 K has been measured by one-photon excitation. The flavoprotein studied was a photoswitchable enzyme, photoactivated adenylyl cyclase. The time course of the spectrum revealed a structural change occurring at a rate of 10(-3) s(-1) around hydrogen bonds at the flavin cofactor binding site.