Oscillatory dynamics protect enzymes and possibly cells against toxic substances.
We have used the oscillating peroxidase-oxidase (PO) reaction as a model system to study how oscillatory dynamics may affect the influence of toxic reaction intermediates on enzyme stability. In the peroxidase-oxidase reaction reactive intermediates, such as hydrogen peroxide, superoxide, and hydroxyl radical are formed. Such intermediates inactivate many cellular macromolecules such as proteins and nucleic acids. These reaction intermediates also react with peroxidase itself to form an inactive enzyme. The fact that the PO reaction shows bistability between an oscillatory and a steady state gives us a unique possibility to compare such inactivation when the system is in one of these two states. We show that inactivation of peroxidase is slower when the system is in an oscillatory state, and using numerical simulations we provide evidence that oscillatory dynamics lower the average concentration of the reactive intermediates.
Hauser
M J
MJ
Institut für Experimentelle Physik, Abteilung Biophysik, Otto-von-Guericke Universität, Postfach 4120, D-39016 Magdeburg, Germany.
Kummer
U
U
Larsen
A Z
AZ
Olsen
L F
LF
D002477:Cells / Q000187:drug effects*; D004798:Enzymes / Q000187:drug effects*; D005609:Free Radicals; D006735:Horseradish Peroxidase / Q000737:chemistry; D017711:Nonlinear Dynamics; D010088:Oxidoreductases / Q000737:chemistry; D010544:Peroxidases / Q000737:chemistry; D011042:Poisons / Q000633:toxicity*
D004798:Enzymes; D005609:Free Radicals; D011042:Poisons; D010088:Oxidoreductases; D006735:Horseradish Peroxidase; D010544:Peroxidases