The peroxidase-oxidase oscillator, a model of biological oscillations, is usually studied in conjunction with the effector molecule, 2,4-dichlorophenol. In this account, we present evidence of the effects of a naturally occurring phenol, tyramine, on the reaction, and also those of the structurally similar 4-aminophenol. Whereas 2,4-dichlorophenol gives rise to sustained oscillations at 40 μM, it was discovered that tyramine promotes damped oscillations at a concentration of 120 μM. Oxidation of NADH was completely inhibited by 4-aminophenol and ascorbate. In separate experiments, the peroxidase-catalyzed ring coupling of tyramine and 4-aminophenol was observed, which in the case of tyramine, may provide an explanation for the damping of oscillations.