Physical Chemistry Chemical Physics

, volume 17 , issue 31 , pages 20056-20060

How far can a single hydrogen bond tune the spectral properties of the GFP chromophore?

H. V. Kiefer ^{1, 2, 3, 4, 5}

Elie Lattouf ^{1, 2, 3, 4, 5}

Natascha W Persen ^{1, 2, 3, 4, 5}

Anastasia V. Bochenkova ^{1, 6}

L P Andersen ¹

Lars H Andersen ^{2, 3, 4, 5}

Hide authors affiliations Show authors affiliations: 6 affiliations

Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark |

Department of Physics and Astronomy

AARHUS UNIVERSITY |

⁴

DK-8000 Aarhus C |

⁵

Denmark |

⁶

Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia |

Publication type: Journal Article

Publication date: 2015-06-23

Royal Society of Chemistry (RSC)

Physical Chemistry Chemical Physics

scimago Q2

wos Q2

SJR: 0.698

CiteScore: 5.3

Impact factor: 2.9

ISSN: 14639076, 14639084

DOI: 10.1039/c5cp02764k

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PubMed ID: 26118481

Physical and Theoretical Chemistry

General Physics and Astronomy

Abstract

Photoabsorption of the hydrogen-bonded complex of a neutral and an anionic Green Fluorescent Protein chromophore has been studied using a new dual-detection approach to action-absorption spectroscopy. Following absorption of one photon, dissociation through a single channel ensures that the full absorption spectrum is measured. Our theoretical account of the spectral shape reveals that the anionic 0-0 transition (464 nm) is blue-shifted compared to that of the wild-type protein (478 nm) due to the stronger H-bond in the dimer, and represents an upper bound for that of the isolated anion. At the same time, the apparent effect of the H-bond for the neutral chromophore is as large as 0.5 eV, red-shifting the absorption maximum of the isolated neutral (340 nm) to that measured in the dimer (393 nm) and various proteins (∼395 nm). This shift results from changes in the topography of potential-energy surfaces in the Franck-Condon region of the H-bonded systems.

Found

3 citations

Bochenkova Anastasia

🥼

PhD in Physics and Mathematics, associate professor

73 publications, 1 202 citations, 118 reviews

h-index: 20

Lomonosov Moscow State University

Research interests

Photochemistry

Quantum Chemistry

1 citation

Kabylda Adil

20 publications, 263 citations, 3 reviews

h-index: 9

Lomonosov Moscow State University

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Kiefer H. V. et al. How far can a single hydrogen bond tune the spectral properties of the GFP chromophore? // Physical Chemistry Chemical Physics. 2015. Vol. 17. No. 31. pp. 20056-20060.

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Kiefer H. V., Lattouf E., Persen N. W., Bochenkova A. V., Andersen L. P., Andersen L. H. How far can a single hydrogen bond tune the spectral properties of the GFP chromophore? // Physical Chemistry Chemical Physics. 2015. Vol. 17. No. 31. pp. 20056-20060.

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