Grateful to see our small contribution to the big story "Illuminating the mechanism and allosteric behavior of NanoLuc luciferase" published in Nature Communications today! @Science_MEDMUNI @sci_muni. Congrats to Loschmidt Laboratories and all the authors!
We investigated the complex mechanism and allosteric behavior of NanoLuc luciferase, combining experimental and computational techniques. Our findings reveal that imidazopyrazinone luciferins bind not only to an intra-barrel catalytic site but also to an allosteric site on the enzyme's surface. Binding at one site prevents simultaneous binding at the other, due to a homotropic negative allostery mechanism. We discovered that restructuring the allosteric site enhances luminescence in the active site, providing insights critical for developing next-generation bioluminescent reporters. Our work elucidates the catalytic mechanism of NanoLuc, involving a radical charge-transfer mechanism, and demonstrates the potential for engineering superior in vivo reporters through allosteric site modification.
We are seeking a talented and motivated candidate to join our research team. Our lab focuses on understanding the molecular mechanisms behind retinal development and disease using human pluripotent stem cells. We specialize in creating retinal organoids, “eye-like” organoids, and other retinal cell types to model eye development and associated disorders, with a particular interest in photoreceptor biology.
Tereza Krivska, my bachelor (!!!) student presenting her data. And my PhD student Francisco Molina Gambin, presenting his BBS syndrome story at ISSCR meeting "Elucidating Principles of Development with Stem Cells" in Vienna in Hofburg
