Fluorescent proteins as singlet oxygen photosensitizers: mechanistic studies in photodynamic inactivation of bacteria

Author(s):  
Rubén Ruiz-González ◽  
John H. White ◽  
Aitziber L. Cortajarena ◽  
Montserrat Agut ◽  
Santi Nonell ◽  
...  

2007 ◽  
Vol 104 (17) ◽  
pp. 7223-7228 ◽  
Author(s):  
T. Maisch ◽  
J. Baier ◽  
B. Franz ◽  
M. Maier ◽  
M. Landthaler ◽  
...  


2010 ◽  
Vol 3 (5-6) ◽  
pp. 319-327 ◽  
Author(s):  
Johannes Regensburger ◽  
Tim Maisch ◽  
Ariane Felgenträger ◽  
Francesco Santarelli ◽  
Wolfgang Bäumler


2014 ◽  
Vol 2 (40) ◽  
pp. 7073-7081 ◽  
Author(s):  
Bo Hu ◽  
Xian Cao ◽  
Keaton Nahan ◽  
Joseph Caruso ◽  
Hong Tang ◽  
...  

A general platform to improve singlet oxygen productionviaresonance coupling between surface plasmon and photosensitizers, and for broad-spectrum photodynamic inactivation of bacteria.







2021 ◽  
Author(s):  
Yuling Xu ◽  
Wei Tuo ◽  
Liang Yang ◽  
Yan Sun ◽  
Chonglu Li ◽  
...  


1976 ◽  
Vol 31 (1-2) ◽  
pp. 29-39 ◽  
Author(s):  
Peter Rosenkranz ◽  
I. Basic Kinetics ◽  
Hartmut Schmidt

The kinetics of the photodynamic desactivation of lysozyme in presence of acridine orange as the sensitizer have been investigated in detail varying oxygen, protein, dye concentration, ionic strength and pH value. The kinetics can be approximately described as an over all pseudo-first- order rate process. Changing the solvent from water to D2O or by quenching experiments in pres­ence of azide ions it could be shown that the desactivation of lysozyme is caused exclusively by singlet oxygen. The excited oxygen occurs via the triplet state of the dye with a rate constant considerably lower than that to be expected for a diffusionally controlled reaction. Singlet oxygen reacts chemically (desactivation, k=2.9 × 107 ᴍ-1 sec-1) and physically (quenching process, k = 4.1 × 108 ᴍ-1sec-1) with the enzyme. The kinetical analysis shows that additional chemical reactions between singlet oxygen and lysozyme would have only little influence on the kinetics of the desactivation as long as their products would be enzymatically active and their kinetical constants would be less than about 1 × 108 ᴍ-1 sec-1.



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