Herein we have engineered a micellar Cu protoporphyrin catalyst that mediates carbon bond activation using peroxide as an electron source. Cu protoporphyrin is a biomimetic model of active site of chloroperoxidase enzyme, which catalyzes the carbon bond halogenation in the presence of a suitable amount of H2O2. The encapsulation of Cu(II) Protoporphyrin IX/L-Cysteine inside of cetyltrimethylammonium bromide micelle increases the rate of chlorination at pH 3. The cited catalyst resists high concentrations of hydrogen peroxide, which is previously reported as a suicide inactivator component of hemo-enzymes. Isothermal Titration Calorimetry (ITC) and Dynamic Light Scattering (DLS) data have revealed the formation of a micellar complex by encapsulation of six Cu(II) proporphyrins within each micelle. Moreover, electrochemical investigations indicate that L-Cysteine increases the intensity of electron transferred due to the formation of self-assembled monolayer on Au electrode. Our results paved a road toward the design of a more robust mimetic catalysis based on Protoporphyrin IX derivatives.