scholarly journals Potentiation of hydrogen peroxide toxicity: From catalase inhibition to stable DNA-iron complexes

2017 ◽  
Vol 773 ◽  
pp. 274-281 ◽  
Author(s):  
Tulip Mahaseth ◽  
Andrei Kuzminov
2018 ◽  
Vol 303 ◽  
pp. 249-255 ◽  
Author(s):  
Syuhei Yamaguchi ◽  
Yuki Miyake ◽  
Keiko Takiguchi ◽  
Daijiro Ihara ◽  
Hidenori Yahiro

2003 ◽  
Vol 8 (1) ◽  
pp. 55-60
Author(s):  
J. Kulys ◽  
K. Kriaučiūnas ◽  
R. Vidžiūnaitė

A mathematical model of kinetics of fungal catalase inhibition with hydroxylamine in presence of substrate (hydrogen peroxide) has been developed. The scheme includes an intermediate formation and slow reversible native enzyme production. The model is based on differential equations of nonstationary kinetics of the enzyme action. The computer simulation was carried out using adaptive Runge-Kuta method. Good satisfactory is achieved if the kinetic constants calculated by modeling nonstationary state of hydrogen peroxide decomposition are used for calculations of inhibition of the catalases at the second phase of inhibition and for kinetics of the intermediate formation, that was determined with stop-flow spectrophotometer.


2004 ◽  
Vol 346 (23) ◽  
pp. 317-332 ◽  
Author(s):  
Georgiy B. Shul'pin ◽  
Galina V. Nizova ◽  
Yuriy N. Kozlov ◽  
Laura Gonzalez Cuervo ◽  
Georg Süss-Fink

1999 ◽  
Vol 344 (2) ◽  
pp. 293-296 ◽  
Author(s):  
Nathaniel G. N. MILTON

Amyloid-β (Aβ) specifically bound purified catalase with high affinity and inhibited catalase breakdown of H2O2. The Aβ-induced catalase inhibition involved formation of the inactive catalase Compound II and was reversible. Catalase ↔ Aβ interactions provide rapid functional assays for the cytotoxic domain of Aβ and suggest a mechanism for some of the observed actions of Aβ plus catalase in vitro.


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