Using data to describe first and second-order kinetics

I completed some graphs of both data sets. Using the model of second-order kinetics (1/A vs t), this was most linear and described the half-life best. Thus, the reactivation seems to be based on second-order kinetics

Since the inactivation is first order and the rectivation is second order, we should be able to explain in terms of the homodimeric activation of the enzyme. The fact that the reactivation is second order implies that the activation process of the enzyme is governed by the assembly of the dimer, since our rate of reactivation would depend on the monomer concentration squared (since it's second-order). The inactivation would be with respect to the concentration of the active enzyme complex, which we can think of as one unit, making the inactivation not depend on the squared value.

Thus, the model would seem to be that two monomers of enzyme will assemble into a homodimer for activity, and heat can dissociate the monomers without peranently damaging them.

I hope that helps!

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