Vibrational assignment of the flavin-cysteinyl adduct in a signaling state of the LOV domain in FKF1.
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.
Kikuchi
Sadato
S
Department of Chemistry and Applied Chemistry, Faculty of Science and Engineering, Saga University, Saga 840-8502, Japan.
Unno
Masashi
M
Zikihara
Kazunori
K
Tokutomi
Satoru
S
Yamauchi
Seigo
S
D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D003460:Crystallization; D003545:Cysteine / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D005415:Flavins / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman / Q000379:methods
D029681:Arabidopsis Proteins; C410504:FKF1 protein, Arabidopsis; D005415:Flavins; D011506:Proteins; D003545:Cysteine