Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

Jason 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 Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

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

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

18 Citations (Scopus)

243 Downloads (Pure)

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
Journal	Journal of Physical Chemistry Letters
Volume	5
Early online date	03 Oct 2014
DOIs	https://doi.org/10.1021/jz5019256
Publication status	Published - 16 Oct 2014

Keywords

absorption, ultra-violet, time dependent density functional theory, femtosecond, gas-phase

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10.1021/jz5019256

Resonantly Enhanced Multiphoton Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore
© 2014 American Chemical Society. This is an open access article published under a Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
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High Harmonic Generation and Attosecond Dynamics in Small Organic Molecules and Biomolecules
Author: Mulholland, P. P., 2019
Supervisor: Dundas, D. (Supervisor)
Student thesis: Doctoral Thesis › Doctor of Philosophy

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Jason Greenwood
- J.Greenwoodqub.acuk
- School of Mathematics and Physics - Reader
- Centre for Light-Matter Interaction (CLMI)
Person: Academic

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title = "Resonantly Enhanced Multi-Photon 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, ultra-violet, time dependent density functional theory, femtosecond, gas-phase",

author = "Jason Greenwood 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.}",

year = "2014",

month = oct,

day = "16",

doi = "10.1021/jz5019256",

language = "English",

volume = "5",

pages = "3588--3592",

journal = "Journal of Physical Chemistry Letters",

issn = "1948-7185",

publisher = "American Chemical Society",

}

Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore. / Greenwood, Jason; Miles, Jordan; De Camillis, Simone; Mulholland, Peter; Zhang, Lijuan; Parkes, Michael A.; Hailes, Helen C.; Fielding, Helen H.

In: Journal of Physical Chemistry Letters, Vol. 5, 16.10.2014, p. 3588-3592.

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

TY - JOUR

T1 - Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

AU - Greenwood, Jason

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, ultra-violet, time dependent density functional theory, femtosecond, gas-phase

U2 - 10.1021/jz5019256

DO - 10.1021/jz5019256

M3 - Article

VL - 5

SP - 3588

EP - 3592

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

SN - 1948-7185

ER -

Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore

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High Harmonic Generation and Attosecond Dynamics in Small Organic Molecules and Biomolecules

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Jason Greenwood

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