ArticleMolecules (Basel, Switzerland)2019
Effect of Protein Conformation and AMP Protonation State on Fireflies' Bioluminescent Emission.
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Molecular Cloning, Biochemical Characterization, and Structural Insights into a Flavonoid-Associated Class II 4-Coumarate:CoA Ligase fromJournal of microbiology and biotechnology · 2026Article
- Mapping the structural dynamics of red- and blue-emitting beetle luciferases revealed by HDX-MS.Life science alliance · 2026Article
- Frontiers in Multiscale Modeling of Photoreceptor Proteins.Photochemistry and photobiology · 2021Review
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Authors and funding
2 authors.
Funding
Abstract
The emitted color in fireflies' bioluminescent systems depends on the beetle species the system is extracted from and on different external factors (pH, temperature…) among others. Controlling the energy of the emitted light (i.e., color) is of crucial interest for the use of such bioluminescent systems. For instance, in the biomedical field, red emitted light is desirable because of its larger tissue penetration and lower energies. In order to investigate the influence of the protein environment and the AMP protonation state on the emitted color, the emission spectra of the phenolate-keto and phenolate-enol oxyluciferin forms have been simulated by means of MD simulations and QM/MM calculations, considering: two different protein conformations (with an open or closed C-terminal domain with respect to the N-terminal) and two protonation states of AMP. The results show that the emission spectra when considering the protein characterized by a closed conformation are blue-shifted compared to the open conformation. Moreover, the complete deprotonation of AMP phosphate group (AMP
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