On the absorption of the phenolatechromophore in the green fluorescent protein—role of individual interactions

Lincke, Kasper; Sølling, Theis I.; Andersen, Lars H.; Klærke, B.; Rahbek, Dennis B.; Rajput, Jyoti; Oehlenschlæger, Christian B; Petersen, Michael; Nielsen, Mogens Brøndsted

doi:10.1039/b920378h

Cited by 16 publications

(6 citation statements)

References 24 publications

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“…The difference of λ abs between 1OH and 1OMe and between 2OH and 2OMe is little or none, revealing a weak H-bonding effect on λ abs . A similar situation was also reported for an intramolecularly H-bonded derivative of p -HBDI …”

supporting

confidence: 82%

Site-Selective Hydrogen-Bonding-Induced Fluorescence Quenching of Highly Solvatofluorochromic GFP-like Chromophores

et al. 2012

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The unconstrained green fluorescence protein (GFP)-like chromophore m-DMABDI displays a high solvatofluorochromicity in aprotic solvents, but the fluorescence is quenched in protic solvents. According to the site-specific intramolecularly hydrogen-bonded analogs 1OH and 2OH, the hydrogen bonding to the carbonyl oxygen is more important than that to the imino nitrogen of the imidazolinone group in the fluorescence quenching.

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supporting

confidence: 82%

Site-Selective Hydrogen-Bonding-Induced Fluorescence Quenching of Highly Solvatofluorochromic GFP-like Chromophores

et al. 2012

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“…The mechanism by which the protein exerts such a large effect on the absorbance remains a mystery. This mystery is further compounded by the observation that the gas-phase absorbance of anionic p O – -BDI anion is actually quite close to the absorbance of the B state of GFP …”

Section: Introductionmentioning

confidence: 99%

“…This mystery is further compounded by the observation that the gasphase absorbance of anionic pO − -BDI anion is actually quite close to the absorbance of the B state of GFP. 6 chromophore is understanding the electronic physics of the chromophore itself, identifying key electronic degrees of freedom that can modulate the spectral properties. One of the key parameters determining the spectra of GFPs is the proton occupancy of the titratable para-alcoholic center.…”

Section: ■ Introductionmentioning

confidence: 99%

Locally-Excited (LE) versus Charge-Transfer (CT) Excited State Competition in a Series of Para-Substituted Neutral Green Fluorescent Protein (GFP) Chromophore Models

Olsen

2014

J. Phys. Chem. B

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In this paper, I provide a characterization of the low-energy electronic structure of a series of para-substituted neutral green fluorescent protein (GFP) chromophore models using a theoretical approach that blends linear free energy relationships (LFERs) with state-averaged complete-active-space self-consistent field (SA-CASSCF) theory. The substituents are chosen to sample the Hammett σ(p) scale from R = F to NH2, and a model of the neutral GFP chromophore structure (R = OH) is included. I analyze the electronic structure for different members of the series in a common complete-active-space valence-bond (CASVB) representation, exploiting an isolobal analogy between active-space orbitals for different members of the series. I find that the electronic structure of the lowest adiabatic excited state is a strong mixture of weakly coupled states with charge-transfer (CT) or locally excited (LE) character and that the dominant character changes as the series is traversed. Chromophores with strongly electron-donating substituents have a CT-like excited state such as expected for a push-pull polyene or asymmetric cyanine. Chromophores with weakly electron-donating (or electron-withdrawing) substituents have an LE-like excited state with an ionic biradicaloid structure localized to the ground-state bridge π bond.

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“…The intrinsic absorption properties of the anion have been studied in ion storage devices through fragmentation induced by photon absorption, known as action spectroscopy. − Several of these measurements have shown that the deprotonated chromophore anion in the gas-phase anion has the same absorption maximum as that of the protein in its anionic form, whereas in solution the spectrum is blue-shifted. This has led to the suggestion that the environment of the chromophore in the protein is similar to that of an isolated chromophore in the gas phase; however, this is a subject of debate.…”

mentioning

confidence: 99%

Resonantly Enhanced Multiphoton Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

Greenwood

Miles

Camillis

et al. 2014

J. Phys. Chem. Lett.

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The photophysics of the green fluorescent protein is governed by the electronic structure of the chromophore at the heart of its β-barrel protein structure. We present the first two-color, resonance-enhanced, multiphoton ionization spectrum of the isolated neutral chromophore in vacuo with supporting electronic structure calculations. We find the absorption maximum to be 3.65 ± 0.05 eV (340 ± 5 nm), which is blue-shifted by 0.5 eV (55 nm) from the absorption maximum of the protein in its neutral form. Our results show that interactions between the chromophore and the protein have a significant influence on the electronic structure of the neutral chromophore during photoabsorption and provide a benchmark for the rational design of novel chromophores as fluorescent markers or photomanipulators.

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On the absorption of the phenolatechromophore in the green fluorescent protein—role of individual interactions

Abstract: Model compounds of the green fluorescent protein (GFP) phenolate chromophore are synthesized and investigated for their intrinsic optical properties by state-of-the-art gas-phase action spectroscopy.

Cited by 16 publications

References 24 publications

Site-Selective Hydrogen-Bonding-Induced Fluorescence Quenching of Highly Solvatofluorochromic GFP-like Chromophores

Site-Selective Hydrogen-Bonding-Induced Fluorescence Quenching of Highly Solvatofluorochromic GFP-like Chromophores

Locally-Excited (LE) versus Charge-Transfer (CT) Excited State Competition in a Series of Para-Substituted Neutral Green Fluorescent Protein (GFP) Chromophore Models

Resonantly Enhanced Multiphoton Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

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