Vibrational Assignment of the Flavin−Cysteinyl Adduct in a Signaling State of the LOV Domain in FKF1

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• 作者：Sadato Kikuchi^† ; ; Masashi Unno*^† ; ^‡ ; ; Kazunori Zikihara^§ ; ; Satoru Tokutomi^§ ; ; Seigo Yamauchi
• 刊名：Journal of Physical Chemistry B
• 出版年：2009
• 出版时间：March 5, 2009
• 年：2009
• 卷：113
• 期：9
• 页码：2913-2921
• 全文大小：325K
• 年卷期：v.113,no.9(March 5, 2009)
• ISSN：1520-5207

文摘

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.