Aminoluciferins extend firefly luciferase bioluminescence into the near-infrared and can be preferred substrates over D-luciferin
Department of Biochemistry and Molecular Pharmacology
Biochemistry | Chemistry
Firefly luciferase adenylates and oxidizes d-luciferin to chemically generate visible light and is widely used for biological assays and imaging. Here we show that both luciferase and luciferin can be reengineered to extend the scope of this light-emitting reaction. D-Luciferin can be replaced by synthetic luciferin analogues that increase near-infrared photon flux > 10-fold over that of D-luciferin in live luciferase-expressing cells. Firefly luciferase can be mutated to accept and utilize rigid aminoluciferins with high activity in both live and lysed cells yet exhibit 10,000-fold selectivity over the natural luciferase substrate. These new luciferin analogues thus pave the way to an extended family of bioluminescent reporters.
DOI of Published Version
J Am Chem Soc. 2014 Sep 24;136(38):13277-82. doi: 10.1021/ja505795s. Epub 2014 Sep 11.Link to article on publisher's site
Journal of the American Chemical Society
Mofford DM, Reddy GR, Miller SC. (2014). Aminoluciferins extend firefly luciferase bioluminescence into the near-infrared and can be preferred substrates over D-luciferin. Morningside Graduate School of Biomedical Sciences Student Publications. https://doi.org/10.1021/ja505795s. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/2048