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Originally published as Biophys J. BioFAST on August 31, 2007.
doi:10.1529/biophysj.107.107128
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Biophysical Journal 94:168-172 (2008)
© 2008 The Biophysical Society

Singlet Oxygen Photosensitization by EGFP and its Chromophore HBDI

Ana Jiménez-Banzo *, Santi Nonell *, Johan Hofkens {dagger} and Cristina Flors {dagger}

* Grup d'Enginyeria Molecular, Institut Químic de Sarrià, Barcelona, Spain; and {dagger} Department of Chemistry and Institute for Nanoscale Physics and Chemistry, Katholieke Universiteit Leuven, Heverlee, Belgium

Correspondence: Address reprint requests to Santi Nonell, E-mail: santi.nonell{at}iqs.url.edu; or Cristina Flors, E-mail: cristina.florsong{at}chem.kuleuven.be.

The photosensitization of reactive oxygen species and, in particular, singlet oxygen by proteins from the green fluorescent protein (GFP) family influences important processes such as photobleaching and genetically targeted chromophore-assisted light inactivation. In this article, we report an investigation of singlet oxygen photoproduction by GFPs using time-resolved detection of the NIR phosphorescence of singlet oxygen at 1275 nm. We have detected singlet oxygen generated by enhanced (E)GFP, and measured a lifetime of 4 µs in deuterated solution. By comparison with the model compound of the EGFP fluorophore 4-hydroxybenzylidene-1,2-dimethylimidazoline (HBDI), our results confirm that the β-can of EGFP provides shielding of the fluorophore and reduces the production of this reactive oxygen species. In addition, our results yield new information about the triplet state of these proteins. The quantum yield for singlet oxygen photosensitization by the model chromophore HBDI is 0.004.




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J. Hendrix, C. Flors, P. Dedecker, J. Hofkens, and Y. Engelborghs
Dark States in Monomeric Red Fluorescent Proteins Studied by Fluorescence Correlation and Single Molecule Spectroscopy
Biophys. J., May 15, 2008; 94(10): 4103 - 4113.
[Abstract] [Full Text] [PDF]


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