Describing Two-Photon Absorptivity of Fluorescent Proteins with a New Vibronic Coupling Mechanism

Drobizhev, Mikhail; Makarov, Nikolay S.; Tillo, Shane; Hughes, Thomas E.; Rebane, Aleksander

doi:10.1021/jp211020k

Cited by 63 publications

(82 citation statements)

References 57 publications

(137 reference statements)

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“…The short-wavelength shift of the 2PA maximum was recently explained by a ''Herzberg-Teller''-type of vibronic coupling, specific only for the 2PA transitions in chromophores whose p-conjugation pattern can resonate between the two limiting forms (18). Therefore this mechanism is strongly facilitated in the case of the anion.…”

Section: Properties Of Nowgfpmentioning

confidence: 99%

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Green Fluorescent Protein with Anionic Tryptophan-Based Chromophore and Long Fluorescence Lifetime

Sarkisyan

Goryashchenko

Lidsky

et al. 2015

Biophysical Journal

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Spectral diversity of fluorescent proteins, crucial for multiparameter imaging, is based mainly on chemical diversity of their chromophores. Recently we have reported, to our knowledge, a new green fluorescent protein WasCFP-the first fluorescent protein with a tryptophan-based chromophore in the anionic state. However, only a small portion of WasCFP molecules exists in the anionic state at physiological conditions. In this study we report on an improved variant of WasCFP, named NowGFP, with the anionic form dominating at 37°C and neutral pH. It is 30% brighter than enhanced green fluorescent protein (EGFP) and exhibits a fluorescence lifetime of 5.1 ns. We demonstrated that signals of NowGFP and EGFP can be clearly distinguished by fluorescence lifetime in various models, including mammalian cells, mouse tumor xenograft, and Drosophila larvae. NowGFP thus provides an additional channel for multiparameter fluorescence lifetime imaging microscopy of green fluorescent proteins.

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Section: Properties Of Nowgfpmentioning

confidence: 99%

“…S1 (inset). Furthermore, the 2PA spectrum of NowGFP can be quantitatively described within the framework of the model as a sum of two shifted and properly normalized 1PA spectral replicas (18) (Fig. S1).…”

Section: Properties Of Nowgfpmentioning

confidence: 99%

Green Fluorescent Protein with Anionic Tryptophan-Based Chromophore and Long Fluorescence Lifetime

Sarkisyan

Goryashchenko

Lidsky

et al. 2015

Biophysical Journal

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“…106 Figure 6 shows an example of the band-shape analysis of mStrawberry fluorescent protein, 106 which results in χ G 1.8. This latter result is below χ G obtained in MD simulations of a similar fluorescent protein.…”

Section: Separate Experimental Measurements Of λmentioning

confidence: 99%

Protein electron transfer: Dynamics and statistics

Matyushov

2013

The Journal of Chemical Physics

121

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A statistical-mechanical analysis on the hypermobile water around a large solute with high surface charge density J. Chem. Phys. 130, 014707 (2009) Electron transfer between redox proteins participating in energy chains of biology is required to proceed with high energetic efficiency, minimizing losses of redox energy to heat. Within the standard models of electron transfer, this requirement, combined with the need for unidirectional (preferably activationless) transitions, is translated into the need to minimize the reorganization energy of electron transfer. This design program is, however, unrealistic for proteins whose active sites are typically positioned close to the polar and flexible protein-water interface to allow inter-protein electron tunneling. The high flexibility of the interfacial region makes both the hydration water and the surface protein layer act as highly polar solvents. The reorganization energy, as measured by fluctuations, is not minimized, but rather maximized in this region. Natural systems in fact utilize the broad breadth of interfacial electrostatic fluctuations, but in the ways not anticipated by the standard models based on equilibrium thermodynamics. The combination of the broad spectrum of static fluctuations with their dispersive dynamics offers the mechanism of dynamical freezing (ergodicity breaking) of subsets of nuclear modes on the time of reaction/residence of the electron at a redox cofactor. The separation of time-scales of nuclear modes coupled to electron transfer allows dynamical freezing. In particular, the separation between the relaxation time of electro-elastic fluctuations of the interface and the time of conformational transitions of the protein caused by changing redox state results in dynamical freezing of the latter for sufficiently fast electron transfer. The observable consequence of this dynamical freezing is significantly different reorganization energies describing the curvature at the bottom of electron-transfer free energy surfaces (large) and the distance between their minima (Stokes shift, small). The ratio of the two reorganization energies establishes the parameter by which the energetic efficiency of protein electron transfer is increased relative to the standard expectations, thus minimizing losses of energy to heat. Energetically efficient electron transfer occurs in a chain of conformationally quenched cofactors and is characterized by flattened free energy surfaces, reminiscent of the flat and rugged landscape at the stability basin of a folded protein.

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“…These modes are known to play an important role in the photophysics of conjugated dyes generally 65,66,[87][88][89][90] and in fluorescent protein chromophores particularly. [91][92][93][94] The relevance of bridge stretching modes to the development of charge-transfer behavior is implicit in Scheme 2. The omission of these modes is in keeping with our current narrow goal of achieving a simple model of the coupling between twisting and charge-transfer behavior; strategies for the incorporation of other important modes are deferred for later work.…”

Section: B Computational Quantum Chemistrymentioning

confidence: 99%

A two-state model of twisted intramolecular charge-transfer in monomethine dyes

Olsen

McKenzie

2012

The Journal of Chemical Physics

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Articles you may be interested inModeling opto-electronic properties of a dye molecule in proximity of a semiconductor nanoparticle J. Chem. Phys. 139, 024105 (2013) A two-state model Hamiltonian is proposed, which can describe the coupling of twisting displacements to charge-transfer behavior in the ground and excited states of a general monomethine dye molecule. This coupling may be relevant to the molecular mechanism of environment-dependent fluorescence yield enhancement. The model is parameterized against quantum chemical calculations on different protonation states of the green fluorescent protein chromophore, which are chosen to sample different regimes of detuning from the cyanine (resonant) limit. The model provides a simple yet realistic description of the charge transfer character along two possible excited state twisting channels associated with the methine bridge. It describes qualitatively different behavior in three regions that can be classified by their relationship to the resonant (cyanine) limit. The regimes differ by the presence or absence of twist-dependent polarization reversal and the occurrence of conical intersections. We find that selective biasing of one twisting channel over another by an applied diabatic biasing potential can only be achieved in a finite range of parameters near the cyanine limit.

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Describing Two-Photon Absorptivity of Fluorescent Proteins with a New Vibronic Coupling Mechanism

Cited by 63 publications

References 57 publications

Green Fluorescent Protein with Anionic Tryptophan-Based Chromophore and Long Fluorescence Lifetime

Green Fluorescent Protein with Anionic Tryptophan-Based Chromophore and Long Fluorescence Lifetime

Protein electron transfer: Dynamics and statistics

A two-state model of twisted intramolecular charge-transfer in monomethine dyes

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