期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 37, 页码 9797-9801出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201404609
关键词
ab initio calculations; action spectroscopy; electron transfer; green fluorescent protein; photophysics
资金
- Carlsberg Foundation
- Villum Foundation
- Danish Research Agency
- FP7 Marie-Curie CIG grant
- RFBR [14-03-00887]
Members of the green fluorescent protein (GFP) family may undergo irreversible phototransformation upon irradiation with UV light. This provides clear evidence for the importance of the higher-energy photophysics of the chromophore, which remains essentially unexplored. By using time-resolved action and photoelectron spectroscopy together with high-level electronic structure theory, we directly probe and identify higher electronically excited singlet states of the isolated para- and meta-chromophore anions of GFP. These molecular resonances are found to serve as a doorway for very efficient electron detachment in the gas phase. Inside the protein, this band is found to be resonant with the quasicontinuum of a solvated electron, thus enhancing electron transfer from the GFP to the solvent. This suggests a photophysical pathway for photoconversion of the protein, where GFP resonant photooxidation in solution triggers radical redox reactions inside these proteins.
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