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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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Published in: | Physical chemistry chemical physics : PCCP 2023-12, Vol.25 (48), p.32868-32874 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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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. |
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ISSN: | 1463-9076 1463-9084 |
DOI: | 10.1039/d3cp04696f |