Excited-state dynamics and fluorescence lifetime of cryogenically cooled green fluorescent protein chromophore anions

Time-resolved action spectroscopy together with a fs-pump probe scheme is used in an electrostatic ion-storage ring to address lifetimes of specific vibrational levels in electronically excited states. Here we specifically consider the excited-state lifetime of cryogenically cooled green fluorescent...

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Bibliographic Details
Published in:Physical chemistry chemical physics : PCCP 2023-12, Vol.25 (48), p.32868-32874
Main Authors: Rasmusssen, Anne P, Pedersen, Henrik B, Andersen, Lars H
Format: Article
Language:English
Subjects:
Anions
Chromophores
Excitation
Internal conversion
Proteins
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Summary:Time-resolved action spectroscopy together with a fs-pump probe scheme is used in an electrostatic ion-storage ring to address lifetimes of specific vibrational levels in electronically excited states. Here we specifically consider the excited-state lifetime of cryogenically cooled green fluorescent protein (GFP) chromophore anions which is systematically measured across the S 0 -S 1 spectral region (450-482 nm). A long lifetime of 5.2 ± 0.3 ns is measured at the S 0 -S 1 band origin. When exciting higher vibrational levels in S 1 , the lifetime changes dramatically. It decreases by more than two orders of magnitude in a narrow energy region ∼250 cm −1 (31 meV) above the 0-0 transition. This is attributed to the opening of internal conversion over an excited-state energy barrier. The applied experimental technique provides a new way to uncover even small energy barriers, which are crucial for excited-state dynamics. The intrinsic fluorescence lifetime and excited state barrier of the green fluorescent protein (GFP) model chromophore HBDI anion are found in the gas-phase by fs-pump pulse measurements.
ISSN:1463-9076
1463-9084
DOI:10.1039/d3cp04696f