The influence of temperature on the oscillatory kinetics of the peroxidase-oxidase reaction was studied theoretically. Assuming Q10=2 for elementary reactions, the effect of multiplying the rate constants of the model by factors between 0.5 and 2 (corresponding to a 10 °C decrease and increase, respectively, of temperature) was investigated. First, the individual rate constants were successively multiplied by 0.5 or 2 while all other rate constants were kept unchanged. This resulted in either a longer or a shorter period, depending on the rate constant being changed. Multiplication by 0.5 or by 2 generally resulted in opposite effects on the period length. However, the absolute value of this deviation differed. Also, the dynamics changed when halving the dimerization rate of NAD+ as wail as when doubling the rate constant for the reduction of ferric peroxidase by NAD+. Next, simulations were performed multiplying all rate constants by one and the same factor, which increased progressively from 0.5 to 2. Intervals were found corresponding to temperature dependency, compensation, and over-compensation, respectively.