Resonantly enhanced multiphoton ionization spectrum of the neutral green fluorescent protein chromophore

Jason B. Greenwood; Jordan Miles; Simone De Camillis; Peter Mulholland; Lijuan Zhang; Michael A. Parkes; Helen C. Hailes; Helen H. Fielding

doi:10.1021/jz5019256

Resonantly enhanced multiphoton ionization spectrum of the neutral green fluorescent protein chromophore

Jason B. Greenwood^*, Jordan Miles, Simone De Camillis, Peter Mulholland, Lijuan Zhang, Michael A. Parkes, Helen C. Hailes, Helen H. Fielding

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	3588-3592
Number of pages	5
Journal	Journal of Physical Chemistry Letters
Volume	5
Issue number	20
DOIs	https://doi.org/10.1021/jz5019256
Publication status	Published - 16 Oct 2014
Externally published	Yes

Keywords

absorption
femtosecond
gas phase
time-dependent density functional theory
ultraviolet

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title = "Resonantly enhanced multiphoton ionization spectrum of the neutral green fluorescent protein chromophore",

abstract = "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.",

keywords = "absorption, femtosecond, gas phase, time-dependent density functional theory, ultraviolet",

author = "Greenwood, {Jason B.} and Jordan Miles and {De Camillis}, Simone and Peter Mulholland and Lijuan Zhang and Parkes, {Michael A.} and Hailes, {Helen C.} and Fielding, {Helen H.}",

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AU - Greenwood, Jason B.

AU - Miles, Jordan

AU - De Camillis, Simone

AU - Mulholland, Peter

AU - Zhang, Lijuan

AU - Parkes, Michael A.

AU - Hailes, Helen C.

AU - Fielding, Helen H.

PY - 2014/10/16

Y1 - 2014/10/16

N2 - 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.

AB - 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.

KW - absorption

KW - femtosecond

KW - gas phase

KW - time-dependent density functional theory

KW - ultraviolet

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DO - 10.1021/jz5019256

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JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

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Resonantly enhanced multiphoton ionization spectrum of the neutral green fluorescent protein chromophore

Abstract

Keywords

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