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Temperature dependence of oxygen evolution through catalase-like activity of horseradish peroxidase

  • Chemical Kinetics and Catalysis
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Abstract

By experimental investigations of the temperature dependence of catalase-like activity of horseradish peroxidase in the temperature range 278–328 K, different kinetic profiles for oxygen evolution were found below and above 298 K. Extension of the model is proposed to account for these observations. By numeric simulations of the reaction kinetics at different temperatures, it was found that enhanced evaporation of molecular oxygen from the reaction solution is the main root through which oxygen is lost at elevated temperatures in laboratory conditions.

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Authors and Affiliations

  1. Faculty of Physical Chemistry, University of Belgrade, Studentski Trg 12-16, 11000, Belgrade, Serbia

    A. Popović-Bijelić & Lj. Kolar-Anić

  2. Center for Multidisciplinary Studies, University of Belgrade Kneza Višeslava 1, 11000, Belgrade, Serbia

    G. Bijelić

  3. Department of Clinical Neuroscience, Karolinska Institute, CMML8:01, 17176, Stockholm, Sweden

    V. Vukojević

Authors
  1. A. Popović-Bijelić
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  2. G. Bijelić
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  3. Lj. Kolar-Anić
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  4. V. Vukojević
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Corresponding author

Correspondence to A. Popović-Bijelić.

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The text was submitted by the authors in English.

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Popović-Bijelić, A., Bijelić, G., Kolar-Anić, L. et al. Temperature dependence of oxygen evolution through catalase-like activity of horseradish peroxidase. Russ. J. Phys. Chem. 81, 1371–1373 (2007). https://doi.org/10.1134/S003602440709004X

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  • DOI: https://doi.org/10.1134/S003602440709004X

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