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Singlet Oxygen Induces Fluorescent Proteins Dimerization
Author(s) -
ValenciaPerez Adriana Z.,
Heyne Belinda
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000505
Subject(s) - singlet oxygen , fluorescence , förster resonance energy transfer , green fluorescent protein , photochemistry , absorption (acoustics) , chemistry , biophysics , oxygen , fluorescence in the life sciences , bimolecular fluorescence complementation , fluorescent protein , materials science , biochemistry , biology , optics , physics , organic chemistry , gene , composite material
Lights out at two: The oxidation of avGFP and EGFP by singlet oxygen not only diminishes their fluorescence emission and changes their absorption properties, but also generates undesired protein aggregation. This could have important consequences in studies in which pairs of fluorescent proteins are used, such as in FRET experiments.