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- The LOV2 domain is a blue light receptor that forms a stable adduct with flavin mononucleotide (FMN), a cofactor crucial for its function.
- Research shows that exchanging FMN with the analogue 5-deazaFMN leads to photochemical changes and the formation of a stable adduct, confirmed through NMR experiments.
- This system exhibits a reliable photocycle, making it a promising alternative to wild-type LOV2 for use in optogenetics, offering easy manipulation in biological applications.
Article Abstract
The LOV2 domain from () is a blue light receptor that undergoes adduct formation with the native flavin mononucleotide (FMN) cofactor [Salomon , , 2000, , 9401]. We report the photochemical changes of LOV2 through cofactor exchange with the FMN analogue 5-deazaFMN. Absorption spectroscopy shows that upon illumination a thermodynamically stable adduct is formed. We were able to confirm the structure of the adduct by introducing C-labelled 5-deazaFMN isotopologues in solution NMR experiments. Dark-adapted state recovery can be photo-induced, providing a photoswitch that is easy to manipulate. The robust photocycle is repeatable without significant loss. Based on the data presented we propose the system as an alternative to wild-type LOV2 for applications in optogenetics.
