Электронный каталог

Статья

Kuznetsova, E.
Characterization of LOV Domain-Ribityllumazine Complex with Blue-Shifted Fluorescence / E.Kuznetsova, V.Borshchevskiy, [a.o.]. – Text : electronic // Biochemical and Biophysical Research Communications. – 2026. – Vol. 836. – P. 154582. – URL: https://doi.org/10.1016/j.bbrc.2026.154582. – Bibliogr.: 51.

Flavin-based fluorescent proteins (FbFPs) are small tags derived from natural LOV domains that can be used for anaerobic imaging. However, their applications are limited due to absence of strongly color-shifted variants. Here, we explore the possibility of reconstituting an FbFP with 6,7-dimethyl-8-ribityllumazine (LUM), an endogenous biosynthetic precursor of riboflavin (RF). We show that CagFbFP binds LUM with low-micromolar affinity (Kd = 9.5 *( 1.1 *mM), forming a fluorescent complex with the excitation maximum at 419 nm and emission maximum at 462 nm. Under blue-light irradiation, CagFbFP-bound LUM is converted irreversibly to 6,7-dimethyllumazine, whereas the more traditional chromophore RF undergoes reversible reduction to hydroquinone form. Crystal structure of the CagFbFP-LUM complex determined at the anisotropic resolution reaching 1.27 Å confirms that the chromophore occupies the canonical flavin-binding pocket. The obtained results pave the way towards engineering of LUM-based FbFP variants with blue-shifted fluorescence emission.



Спец.(статьи,препринты) = С 44 г - Физико-химические методы анализа элементов. Анализ с помощью ядерных методов
Спец.(статьи,препринты) = 28.0 - Биология$
ОИЯИ = ОИЯИ (JINR)2026