Vibrational Assignment of the Flavin-Cysteinyl Adduct in a Signaling State of the LOV Domain in FKF1
Vibrational Assignment of the Flavin-Cysteinyl Adduct in a Signaling State of the LOV Domain in FKF1
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DOI：
10.1021/jp808399f
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发表时间：
2009-03-05
影响因子：
3.3
通讯作者：
Yamauchi, Seigo
中科院分区：
文献类型：
--
作者：
Kikuchi, Sadato;Unno, Masashi;Yamauchi, Seigo
LOV结构域属于PAS结构域超家族，存在于从古细菌到真核生物的多种传感蛋白中，它们以非共价方式结合单个黄素单核苷酸作为发色团。我们报道了拟南芥FKF1中LOV结构域暗态的拉曼光谱。光谱也测量了信号状态，其中半胱氨酸-黄素加合物在光照射下形成。大多数观测到的拉曼带都是在使用密度泛函理论的正模计算的基础上分配的。讨论了对LOV域红外光谱分析的启示。这一综合任务为今后利用振动光谱研究LOV域中的光循环机制提供了一个令人满意的框架。
LOV domains belong to the PAS domain superfamily, which are found in a variety of sensor proteins in organism ranging from archaea to eukaryotes, and they noncovalently bind a single flavin mononucleotide as a chromophore. We report the Raman spectra of the dark state of LOV domain in FKF1 from Arabidopsis thaliana. Spectra have been also measured for the signaling state, where a cysteinyl-flavin adduct is formed upon light irradiation. Most of the observed Raman bands are assigned on the basis of normal mode calculations using a density functional theory. We also discuss implication for the analysis of the infrared spectra of LOV domains. The comprehensive assignment provides a satisfactory framework for future investigations of the photocycle mechanism in LOV domains by vibrational spectroscopy.