The allosteric reaction of protein kinase A (PKA) upon binding of cyclic AMP (cAMP) is revealed with anelectrochemical technique through the redox current change of an electrochemically active marker. The different effectof cAMP's regulation at a distinct concentration level is obtained in this system. The influence of structural analoguesis also examined with respect to the affinity and special selectivity. This study presents an electrochemical approachto the rapid and sensitive investigation of the protein-ligand interaction in the signal transduction networks.