As the magenta simulated plot in Figure still does not completely superimpose to the data, we considered that it could be due to the uncertainty in the selected values of k3 and kred (the latter being moreover recovered from a previous enzymatic study performed with menadione but not with the 1,4-NQ). To experimentally access the value of these two rate constants, we have performed redox cycling experiments (Loop 2) by mixing a fixed concentration of DI (10 nM) and NADH (250 µM) with different concentrations of 1,4-NQ and then monitoring the NADH absorbance decay (see graph A in Figure ). From the results reported in Figure and analyzed in details in SI, we were able to estimate the values of k3 = (5 -8) × 10 4 M -1 •s -1 and kred = (1.5 -0.8) × 10 8 M -1 •s -1 with a reasonably good degree of confidence. We thus considered these new values in our simulations and we succeeded to obtain an almost perfect agreement between the simulated calibration plot and the and), while the solid lines are the theoretical plots predicted from numerical simulations of the autocatalytic set presented in Scheme 3. The parameters used for each simulated plots are those reported in Table according to the following code color: (green) entry 2, (magenta) entry 3, (bleu) entry 4, and (orange) entry 5.