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1976 (1)
1Author    I. Basic, KineticsHartmut Schmidt, Peter RosenkranzRequires cookie*
 Title    On the Mechanism of the Acridine Orange Sensitized Photodynamic Inactivation of Lysozyme  
 Abstract    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 D20 or by quenching experiments in pres­ ence 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 x 107 M -1 sec-1) and physically (quenching process, k = 4.1 x 108 m — 1 sec-J) with the enzyme. The kinetical analysis shows that additional chemical reac­ tions 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 x 1 0 8 m -1 sec-1. 
  Reference    (Z. Naturforsch. 31c, 29 [1976]; received July 7/September 19 1975) 
  Published    1976 
  Keywords    Photodynamic Effect, Singlet Oxygen, Lysozyme, Acridine Orange, Kinetics 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0029.pdf 
 Identifier    ZNC-1976-31c-0029 
 Volume    31