Turning on and off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations

Alexey M. Bogdanov, Atanu Acharya, Anastasia V. Titelmayer, Anastasia V. Mamontova, Ksenia B. Bravaya, Anatoly B. Kolomeisky, Konstantin A. Lukyanov, Anna I. Krylov

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4807-4817
Number of pages11
JournalJournal of the American Chemical Society
Volume138
Issue number14
DOIs
StatePublished - Apr 27 2016
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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