Origin of the Intrinsic Fluorescence of the Green Fluorescent Protein

Svendsen, Annette; Kiefer, Hjalte V.; Pedersen, H. B.; Bochenkova, Anastasia V.; Andersen, Lars H.

doi:10.1021/jacs.7b04987

Cited by 87 publications

(106 citation statements)

References 28 publications

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“…High structural and color diversity of these compounds, as well as their small size, high hydrophilicity, and simple synthetic protocols make them attractive fluorogenic partners . Most chromophores are non‐fluorescent in solution due to the mobility of their benzylidene fragment which can dissipate their excited‐state energy . However, they become highly emissive when the flexible substituent is fixed by an external influence or by an internal lock .…”

Section: Figurementioning

confidence: 99%

“…[9] Most chromophores are non-fluorescent in solution due to the mobility of their benzylidene fragment which can dissipate their excited-state energy. [10] However, they becomeh ighly emissive when the flexible substituenti s fixed by an externali nfluence [11] or by an internal lock. [12] Previously they weres uccessfully used as fluorogens for various proteins, [13] nucleic acids, [14] and whole cell organelles.…”

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confidence: 99%

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Red‐Shifted Substrates for FAST Fluorogen‐Activating Protein Based on the GFP‐Like Chromophores

Povarova

Zaitseva

Балеева

et al. 2019

Chemistry A European J

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A genetically encoded fluorescent tag for live cell microscopy is presented. This tag is composed of previously published fluorogen‐activating protein FAST and a novel fluorogenic derivative of green fluorescent protein (GFP)‐like chromophore with red fluorescence. The reversible binding of the novel fluorogen and FAST is accompanied by three orders of magnitude increase in red fluorescence (580–650 nm). The proposed dye instantly stains target cellular proteins fused with FAST, washes out in a minute timescale, and exhibits higher photostability of the fluorescence signal in confocal and widefield microscopy, in contrast with previously published fluorogen:FAST complexes.

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Section: Figurementioning

confidence: 99%

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confidence: 99%

Red‐Shifted Substrates for FAST Fluorogen‐Activating Protein Based on the GFP‐Like Chromophores

Povarova

Zaitseva

Балеева

et al. 2019

Chemistry A European J

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“…1, R=H) that is anchored, covalently and via a hydrogen-bonded network, to the protein that is wrapped around it in a β-barrel structure. [1][2][3][4][5] Although the isolated deprotonated chromophore is barely fluorescent in the gas-phase or solution, at biological temperatures, [6][7][8] some difluoro-and dimethoxy-substituted analogues (Fig. 1, R=F and R=OMe, respectively) have been shown to become fluorescent when bound to specific ribonucleic acid (RNA) sequences.…”

Section: Introductionmentioning

confidence: 99%

Photoelectron Imaging and Quantum Chemistry Study of Phenolate, Difluorophenolate, and Dimethoxyphenolate Anions

et al. 2019

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Phenolates and their substituted analogues are important molecular motifs in many biological molecules, including the family of fluorescent proteins based on green fluorescent protein. We have used a combination of anion photoelectron velocity-map imaging measurements and quantum chemistry calculations to probe the electronic structure of the phenolate anion and difluoro-and dimethoxy-substituted analogues. We report vertical detachment energies (VDEs) and quantify the photoelectron angular distributions. The VDEs for phenolate (2.26 ± 0.03 eV, 3.22 ± 0.02 eV) are in agreement with high-resolution measurements, whereas the values for the substituted analogues (2.61 ± 0.03 eV for difluorophenolate; ∼ 2.35 eV for dimethoxyphenolate) are new measurements. We also report adiabatic excitation energies (AEEs) of anion resonances and discuss their contributions to the overall photoelectron angular distributions. The AEE of the lowest lying resonance in phenolate (∼ 3.36 eV) is consistent with previous measurements, whereas the value for the next resonance (∼ 3.7 eV) is a new measurement. The AEEs of the resonances in the substituted analogues (∼ 3.74 eV for difluorophenolate; ∼ 3.4 eV and 3.74 eV for dimethoxyphenolate) are new measurements.

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“…The S 1 state of HDBI -has been the focus of a large number of gas-phase studies. 13,19,31,[33][34][35][36][37] A very insightful picture of the electronic structure of the S 1 state was provided by Bravaya et al, who rationalised the energetic shifts in different coloured photoactive proteins using a 3-centre allyl radical in a simple Hückel framework and a particle in the box model. 38 More recently, experimental and computational work has been directed to the higher-lying excited states in the UV spectral region.…”

Section: Introductionmentioning

confidence: 99%

Chromophores of chromophores: a bottom-up Hückel picture of the excited states of photoactive proteins

Anstöter

Dean

Verlet

2017

Phys. Chem. Chem. Phys.

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Citation for published item:enst¤ oterD gte F nd henD ghrlie F nd erletD tn F F @PHIUA 9ghromophores of hromophores X ottomEup r¤ ukel piture of the exited sttes of phototive proteinsF9D hysil hemistry hemil physisFD IW @RRAF ppF PWUUPEPWUUWF Further information on publisher's website: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. Here, we present a reductionist approach to gain fundamental insight into the evolution of electronic structure as the chromophore increases in complexity from phenolate to that in GFP. Using frequency-and angle-resolved photoelectron spectroscopy, in combination with electronic structure theory, the onset of excited states that are responsible for the characteristic spectroscopic features in biochromophores are determined. A comprehensive, yet intuitive picture of the effect of phenolate functionalisation is developed based on simple Hückel theory. Specifically, the first two bright excited states can be constructed from a linear combination of molecular orbitals localised on the phenolate and para-substituent groups. This essential interaction is first observed for p-vinyl-phenolate. This bottom-up approach offers a readily accessible framework for the design of photoactive chromophores.

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Origin of the Intrinsic Fluorescence of the Green Fluorescent Protein

Cited by 87 publications

References 28 publications

Red‐Shifted Substrates for FAST Fluorogen‐Activating Protein Based on the GFP‐Like Chromophores

Red‐Shifted Substrates for FAST Fluorogen‐Activating Protein Based on the GFP‐Like Chromophores

Photoelectron Imaging and Quantum Chemistry Study of Phenolate, Difluorophenolate, and Dimethoxyphenolate Anions

Chromophores of chromophores: a bottom-up Hückel picture of the excited states of photoactive proteins

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