Ultrafast Excited State Relaxation of the Chromophore of the Green Fluorescent Protein

Litvinenko, K. L.; Webber, Naomi M.; Meech, Stephen R.

doi:10.1246/bcsj.75.1065

Cited by 29 publications

(56 citation statements)

References 27 publications

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“…There have been many studies on the denatured GFPC15, 16 and a model compound. 17–22 The first (398 nm) and second (478 nm) peaks were assigned to the neutral (A‐form) and anionic forms (B‐form), respectively. 17, 19 A Raman spectroscopic study17 with a model compound in solution showed that the chromophore has two macroscopic p K a values of 1.8 and 8.2, which are attributed to ionization of the imidazolinone‐ring nitrogen and the phenolic hydroxyl group, respectively.…”

Section: Introductionmentioning

confidence: 99%

Electronic excitations of the green fluorescent protein chromophore in its protonation states: SAC/SAC‐CI study

et al. 2003

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Abstract:Two ground-state protonation forms causing different absorption peaks of the green fluorescent protein chromophore were investigated by the quantum mechanical SAC/SAC-CI method with regard to the excitation energy, fluorescence energy, and ground-state stability. The environmental effect was taken into account by a continuum spherical cavity model. The first excited state, HOMO-LUMO excitation, has the largest transition moment and thus is thought to be the source of the absorption. The neutral and anionic forms were assigned to the protonation states for the experimental A-and B-forms, respectively. The present results support the previous experimental observations.

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Section: Introductionmentioning

confidence: 99%

Electronic excitations of the green fluorescent protein chromophore in its protonation states: SAC/SAC‐CI study

et al. 2003

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“…The suggestion that changes in protein structure can stabilise the A* state is supported by the blGFP A* decay, which occurs on a much longer time scale than for S65T (Figure 4). Thus, these data show that radiationless decay of the A* form (which most likely arises from internal conversion following excited state structural reorganisation (41,42)) can be suppressed by mutagenesis. However, the origin of the stabilisation is not definitively determined.…”

Section: Resultsmentioning

confidence: 71%

Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire

Stoner-Ma¹,

Jaye²,

Ronayne³

et al. 2008

Chemical Physics

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Two blue absorbing and emitting mutants (S65G/T203V/E222Q and S65T at pH 5.5) of the green fluorescent protein (GFP) have been investigated through ultrafast time resolved infra-red (TRIR) and fluorescence spectroscopy. In these mutants, in which the excited state proton transfer reaction observed in wild type GFP has been blocked, the photophysics are dominated by the neutral A state. It was found that the A* excited state lifetime is short, indicating that it is relatively less stabilised in the protein matrix than the anionic form. However, the lifetime of the A* state can be increased through modifications to the protein structure. The TRIR spectra show that a large shifts in protein vibrational modes on excitation of the A* state occurs in both these GFP mutants. This is ascribed to a change in H-bonding interactions between the protein matrix and the excited state.

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“…Several groups have studied the excited state dynamics of wtGFP [58][59][60][61][62][63]. These led to the conclusion that the two visible absorption bands of the wtGFP correspond to protonated and deprotonated ground-state conformations, while upon photoexcitation the acid form A rapidly deprotonates to form the B form.…”

Section: 41mentioning

confidence: 99%

“…While previous time-resolved studies of GFP have focused on emission decay at short times up to 150 ps [58][59][60][61][62][63] Huppert et al have focused on fluorescence at longer times (up to 10 ns). Using the TCSPC technique with a dynamic range of about 4 decades and extending the monitoring range of the emission to much longer times, they find that the fluorescence decay of R*OH is nonexponential up to 10 ns.…”

Section: 41mentioning

confidence: 99%

“…Isolated synthetic GFP and its derivatives do not fluoresce outside the b-barrel at room temperature due to very effective internal conversion related to isomerization along the double bond [59][60][61][62][63]. Deep understanding of the photophysics of these dyes as well as synthesis of their fluorescence derivatives capable of ESPT are our immediate goals.…”

Section: 41mentioning

confidence: 99%

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Design and Implementation of “Super” Photoacids

Tolbert

Solntsev

2006

Hydrogen‐Transfer Reactions

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Electron and proton transfer (see Eqs. (13.1) and (13.2), involve obvious similarities. When the starting materials are neutral, both result in the formation of charge and in the necessity for separation of charge to stabilize the product states. In principle, both can occur in the ground state, but transfer that is exoergic only in the excited state allows the use of time-resolved spectroscopic techniques to determine the details of solvation and structural reorganization. For electron transfer, the development of such techniques and the accompanying theoretical rationale, most especially the Marcus theory, has been one of the triumphs of modern mechanistic chemistry.The relationship between driving force and proton transfer has been much more elusive despite considerable evidence that the vast photosynthetic electron transfer machinery mainly exists to set up a charge gradient to drive proton transfer. This is due to a combination of two factors. First, there is a vast reservoir of readily available materials with which to examine electron transfer. Second, the relationship between rates and driving force for electron transfer, based upon the excitation energies and the relevant redox potentials (the Rehm-Weller equation [1]) is reasonably straightforward. In contrast, the relationship between rates and driving force for excited-state pK a * ¼ pK a À DE o;o =2: 3RT (13.3) proton transfer (based upon relative pK a s and calculated through the Förster equation, Eq. (13.3) [2]) is less straightforward. For instance, the existence of a so-called "inverted" region for proton transfer has been the subject of much controversyHydrogen-Transfer Reactions. Edited by

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Ultrafast Excited State Relaxation of the Chromophore of the Green Fluorescent Protein

Cited by 29 publications

References 27 publications

Electronic excitations of the green fluorescent protein chromophore in its protonation states: SAC/SAC‐CI study

Electronic excitations of the green fluorescent protein chromophore in its protonation states: SAC/SAC‐CI study

Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire

Design and Implementation of “Super” Photoacids

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