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- W4383761497 abstract "By time-resolved action spectroscopy of cryogenically cooled molecular ions, we have achieved a remarkable vibrational resolution in the photoresponse of the deprotonated green fluorescent protein (GFP) chromophore, a key molecular unit in the bioimaging of living cells. We define four characteristic spectral regions of the S0-S1 band with competing electronic and nuclear decay channels. We determine the energy barrier toward internal conversion to be ∼250 cm-1. This inhibits internal conversion and hence statistical fragmentation near the S0-S1 band origin, which is identified at 481.51 ± 0.15 nm (20768 ± 6 cm-1). The origin is red-shifted by only 221 cm-1 compared to that of wild-type GFP at 77 K. This, together with a striking agreement between the vibronic profiles of the protein and its chromophore, suggests their similar photophysics. In combination with theory, the data reveal the coexistence of mutually energy-borrowing mechanisms between nuclei and electrons mediated by specific vibrational modes." @default.
- W4383761497 created "2023-07-11" @default.
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- W4383761497 date "2023-07-10" @default.
- W4383761497 modified "2023-09-25" @default.
- W4383761497 title "High-Resolution Spectroscopy and Selective Photoresponse of Cryogenically Cooled Green Fluorescent Protein Chromophore Anions" @default.
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- W4383761497 doi "https://doi.org/10.1021/acs.jpclett.3c01452" @default.
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