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Modelling the Decamerisation Cycle of PRDX1 and the Inhibition-like Effect on Its Peroxidase Activity.

Christopher J Barry1, Ché S Pillay2, Johann M Rohwer1

  • 1Laboratory for Molecular Systems Biology, Department of Biochemistry, Stellenbosch University, Stellenbosch 7600, South Africa.

Antioxidants (Basel, Switzerland)
|September 28, 2023
PubMed
Summary

Peroxiredoxins are key in reactive oxygen species detoxification. This study models their dimer-to-decamer transition, revealing its impact on enzyme activity and resolving discrepancies in existing models.

Keywords:
enzyme kineticshydrogen peroxideisothermal titration calorimetryoligomerisationparameter estimationperoxiredoxinquantitative redox biologysystems biology

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Area of Science:

  • Biochemistry
  • Enzymology
  • Cellular Redox Biology

Background:

  • Peroxiredoxins (PRDXs) are crucial for reactive oxygen species (ROS) detoxification.
  • The dimer-to-decamer transition significantly alters PRDX activity but is understudied due to limited kinetic data and theoretical frameworks.
  • Existing kinetic models often overlook this oligomeric transition.

Purpose of the Study:

  • To determine the kinetic parameters for the human PRDX1 dimer-to-decamer transition.
  • To develop a simplified theoretical framework for modeling the PRDX decamer oxidation cycle.
  • To investigate the impact of the dimer-decamer transition on PRDX function in vitro and in vivo.

Main Methods:

  • Analysis of published isothermal titration calorimetry (ITC) data to derive association and dissociation rate constants.
  • Development of a reduced reaction scheme for modeling the PRDX decamer oxidation.
  • Simulation of peroxidase competition and NADPH-oxidation assays.
  • Integration of dimer-decamer kinetics into an established in vivo model of PRDX2 in erythrocytes.

Main Results:

  • Association and dissociation rate constants for human PRDX1 dimer-decamer transition were determined (0.050 µM⁻⁴·s⁻¹ and 0.055 s⁻¹, respectively).
  • The dimer-decamer transition was found to inhibit peroxidase activity in simulated assays.
  • Incorporating this transition into an in vivo PRDX2 model significantly improved the reconciliation of experimental and simulated responses to hydrogen peroxide.

Conclusions:

  • The dimer-to-decamer transition is a critical, underappreciated factor in peroxiredoxin kinetics and function.
  • The developed modeling approach simplifies the study of PRDX decamer oxidation.
  • Accounting for PRDX oligomerization resolves discrepancies between experimental observations and existing kinetic models, enhancing our understanding of cellular redox homeostasis.