This model is described in the article: The mechanism of catalase action. II. Electric analog computer studies. Britton Chance, David S Greenstein, Joseph Higgins, CC Yang, Arch Biochem. 1952 37:322-39. PubmedID: 14953444 Summary: An electric analog computer has been constructed for a study of the kinetics of catalase action. This computer gives results for the formation and disappearance of the catalase-hydrogen peroxide complex that are in good agreement with the experimental data. The computer study verifies an approximate method for the computation of the velocity constant for the combination of hydrogen peroxide and catalase and justifies the simple formula used previously to compute the velocity constant for the reaction of the catalase-hydrogen peroxide complex with donor molecules. Finally, the computer data show that the binding of peroxide to catalase is a practically irreversible reaction. The reaction of the enzyme-substrate complex, p, with the electron donor, a, is bimolecular, although in the article, as a is assumed to be constant, it is modelled using an apparent rate constant consisting of the product of the rate constant, k4, and the concentration of a. In this implementation, the concentration of a is set to 1 and the value of k4 just adapted so that the product equals the values given for k4*a in the article. The specific parameter values are taken from Fig 3. The graphs do not exactly match those in the paper, this may be due to the different simulators used.
enzyme-substrate complex ES (catalase - hydrogen peroxide)