Masuda Shinji, Hasegawa Koji, Ono Taka-Aki
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-5801, Japan.
FEBS Lett. 2005 Aug 15;579(20):4329-32. doi: 10.1016/j.febslet.2005.06.069.
A sensor of blue light using FAD (BLUF) protein is a flavin adenine dinucleotide (FAD) based new class blue-light sensory flavoprotein. The BLUF domain of AppA was reconstituted in vitro from apoprotein and flavin adenine dinucleotide, flavin adenine mononucleotide or riboflavin. The light-induced FTIR spectra of the domain reconstituted from various flavins and the 13C-labeled apoprotein showed that identical light-induced structural changes occur in both the flavin chromophore and protein for the signaling state in all of the reconstituted holoproteins. The results showed that an adenosine 5'-dinucleotide moiety is not required for signaling-state formation in a BLUF domain.
一种使用黄素腺嘌呤二核苷酸(FAD)的蓝光传感器(BLUF)蛋白是一种基于黄素腺嘌呤二核苷酸的新型蓝光感应黄素蛋白。AppA的BLUF结构域在体外由脱辅基蛋白与黄素腺嘌呤二核苷酸、黄素腺嘌呤单核苷酸或核黄素重构而成。由各种黄素和13C标记的脱辅基蛋白重构的结构域的光诱导傅里叶变换红外光谱表明,在所有重构的全蛋白中,黄素发色团和蛋白质在信号状态下都会发生相同的光诱导结构变化。结果表明,腺苷5'-二核苷酸部分对于BLUF结构域中信号状态的形成并非必需。