Abstract:
:The modifications induced by reactive oxygen species (ROS) on fluorescent proteins (FPs) may have important implications for live cell fluorescence imaging. Using quantitative gamma-radiolysis, we have studied the ROS-induced biochemical and photophysical perturbations on recombinant cyan fluorescent protein (CFP). After oxidation by the OH radical, the protein displays a modified RP-HPLC elution profile, while the CFP fluorescence undergoes pronounced decreases in intensity and lifetime, without changes in its excitation and emission spectra. Meanwhile, the Förster resonant energy transfer (FRET) between the single W(57) and the chromophore remains unperturbed. These results rule out a direct oxidation of the CFP chromophore and of W(57) as well as major changes in the protein 3D structure, but show that new fluorescent forms associated to a higher level of dynamic quenching have been generated. Thus, strict in situ controls are required when CFP is to be used for FRET studies in situations of oxidative activity, or under strong illumination.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Alvarez L,Levin CH,Merola F,Bizouarn T,Pasquier H,Baciou L,Rusconi F,Erard Mdoi
10.1111/j.1751-1097.2009.00617.xsubject
Has Abstractpub_date
2010-01-01 00:00:00pages
55-61issue
1eissn
0031-8655issn
1751-1097pii
PHP617journal_volume
86pub_type
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