ArticleScientific reports2012
Primary role of the chromophore bond length alternation in reversible photoconversion of red fluorescence proteins.
Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The role of the correlated motion(s) of the chromophore in photoswitching of green and red forms of the photoconvertible fluorescent protein mSAASoti.Scientific reports · 2024Article
- Energetic Basis and Design of Enzyme Function Demonstrated Using GFP, an Excited-State Enzyme.Journal of the American Chemical Society · 2022Article
- Multiphoton Bleaching of Red Fluorescent Proteins and the Ways to Reduce It.International journal of molecular sciences · 2022Article
- QM/MM Investigation of the Spectroscopic Properties of the Fluorophore of Bacterial Luciferase.Journal of chemical theory and computation · 2021Article
- A novel method to accurately locate and count large numbers of steps by photobleaching.Molecular biology of the cell · 2016Article
- Long- and Short-Range Electrostatic Fields in GFP Mutants: Implications for Spectral Tuning.Scientific reports · 2015Article
- Inferring diffusion dynamics from FCS in heterogeneous nuclear environments.Biophysical journal · 2015Article
- Femtosecond lasing from a fluorescent protein in a one dimensional random cavity.Biomedical optics express · 2015Article
- Multiphoton photochemistry of red fluorescent proteins in solution and live cells.The journal of physical chemistry. B · 2014Article
- Molecular structure-optical property relationships for a series of non-centrosymmetric two-photon absorbing push-pull triarylamine molecules.Scientific reports · 2014Article
- Strengths and weaknesses of recently engineered red fluorescent proteins evaluated in live cells using fluorescence correlation spectroscopy.International journal of molecular sciences · 2013Article
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Authors and funding
10 authors.
Funding
Abstract
Rapid photobleaching of fluorescent proteins can limit their use in imaging applications. The underlying kinetics is multi-exponential and strongly depends on the local chromophore environment. The first, reversible, step may be attributed to a rotation around one of the two exocyclic C-C bonds bridging phenol and imidazolinone groups in the chromophore. However it is not clear how the protein environment controls this motion - either by steric hindrances or by modulating the electronic structure of the chromophore through electrostatic interactions. Here we study the first step of the photobleaching kinetics in 13 red fluorescent proteins (RFPs) with different chromophore environment and show that the associated rate strongly correlates with the bond length alternation (BLA) of the two bridge bonds. The sign of the BLA appears to determine which rotation is activated. Our results present experimental evidence for the dominance of electronic effects in the conformational dynamics of the RFP chromophore.
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