Turning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations
| Autor: | Konstantin A. Lukyanov, Anastasia V. Mamontova, Anna I. Krylov, Anastasia V. Titelmayer, Anatoly B. Kolomeisky, Atanu Acharya, Ksenia B. Bravaya, Alexey M. Bogdanov |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Bromides Models Molecular Green Fluorescent Proteins Stacking Plasma protein binding 010402 general chemistry Photochemistry 01 natural sciences Biochemistry Catalysis Photoinduced electron transfer Green fluorescent protein 03 medical and health sciences Electron transfer Fluorides Colloid and Surface Chemistry Bacterial Proteins Chlorides Humans chemistry.chemical_classification Chemistry General Chemistry Chromophore Electron acceptor Iodides Photochemical Processes Fluorescence 0104 chemical sciences Molecular Docking Simulation Luminescent Proteins 030104 developmental biology HEK293 Cells Microscopy Fluorescence Mutation Mutagenesis Site-Directed Thermodynamics Tyrosine Oxidation-Reduction Protein Binding |
| Zdroj: | Journal of the American Chemical Society. 138(14) |
| ISSN: | 1520-5126 |
| Popis: | Photoinduced electron transfer in fluorescent proteins from the GFP family can be regarded either as an asset facilitating new applications or as a nuisance leading to the loss of optical output. Photooxidation commonly results in green-to-red photoconversion called oxidative redding. We discovered that yellow FPs do not undergo redding; however, the redding is restored upon halide binding. Calculations of the energetics of one-electron oxidation and possible electron transfer (ET) pathways suggested that excited-state ET proceeds through a hopping mechanism via Tyr145. In YFPs, the π-stacking of the chromophore with Tyr203 reduces its electron-donating ability, which can be restored by halide binding. Point mutations confirmed that Tyr145 is a key residue controlling ET. Substitution of Tyr145 by less-efficient electron acceptors resulted in highly photostable mutants. This strategy (i.e., calculation and disruption of ET pathways by mutations) may represent a new approach toward enhancing photostability of FPs. |
| Databáze: | OpenAIRE |
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