Oxidation of Horseradish Peroxidase (HRP) to Compound I (CpI) induces release of the protein from adsorbing silica surfaces. Adsorption and desorption can be modulated by changes in concentration of hydrogen peroxide in solution in contact with the adsorber. Coupling of the HRP adsorption-desorption cycles to the chemistry of the peroxidase in bulk solution by oscillations in concentration of hydrogen peroxide is postulated as a plausible explanation for a qualitative change in the dynamics of the peroxidase oscillator at low concentrations of the enzyme. We hypothesize that the relative change in the HRP concentration in solution will be most pronounced at low concentrations of the enzyme and high reactor surface-to-volume ratio.