Synthesis and Characterization of the Structure of Neutral Flavin Radicals in Solution
Presentation Type
Poster
Faculty Advisor
Johannes Schelvis
Access Type
Event
Start Date
26-4-2024 2:15 PM
End Date
26-4-2024 3:15 PM
Description
Cryptochromes and photolyases are very similar proteins that serve as signaling proteins and in DNA repair, respectively. These flavoproteins rely on the flavin chromophore to absorb light to carry out their function. Despite significant knowledge about these proteins, less is known about how the flavin cofactor's function is affected by the protein environment. It is also unclear whether structural differences between riboflavin, FMN and FAD affect their ability to function under these conditions. The neutral radical flavin is an important but yet little studied intermediate in the functional cycle of cryptochromes and photolyases. To explore this issue, riboflavin, FMN, and FAD are methylated to stabilize their neutral radical state. Regardless of whether riboflavin, FAD or FMN was used, the radical is able to form, suggesting that the flavin structure is not a limiting factor. This finding suggests that other factors, like pH, protein environment or substrate binding may have more influence on the flavin's function in these proteins.
Synthesis and Characterization of the Structure of Neutral Flavin Radicals in Solution
Cryptochromes and photolyases are very similar proteins that serve as signaling proteins and in DNA repair, respectively. These flavoproteins rely on the flavin chromophore to absorb light to carry out their function. Despite significant knowledge about these proteins, less is known about how the flavin cofactor's function is affected by the protein environment. It is also unclear whether structural differences between riboflavin, FMN and FAD affect their ability to function under these conditions. The neutral radical flavin is an important but yet little studied intermediate in the functional cycle of cryptochromes and photolyases. To explore this issue, riboflavin, FMN, and FAD are methylated to stabilize their neutral radical state. Regardless of whether riboflavin, FAD or FMN was used, the radical is able to form, suggesting that the flavin structure is not a limiting factor. This finding suggests that other factors, like pH, protein environment or substrate binding may have more influence on the flavin's function in these proteins.