Introduction: Heme peroxidases are ubiquitous in nature. They exhibit a variety of functions ranging from catalyzing oxidation reactions to defending against pathogens, synthesis of prostanoids, and reducing peroxide concentration. Horseradish peroxidase (HRP, Scheme 1a) is highly valued by chemical industry for its ability to oxidize organic molecules using hydrogen peroxide as oxidant. It is also being explored as a potential solution for decontaminating wastewater. The remarkable activity of peroxidases is attributed to the generation of compound I and compound II, versatile high-valent oxidants that result from the reaction of peroxides at a histidine-bound ferric heme site, Scheme 1b. Scientists have invested significant efforts to develop functional mimics of these enzymes, such as Fe-TAML, Fe-porphyrin derivatives, and heme-peptide complexes, as well as utilizing various other biological constructs. Despite notable peroxidase activity exhibited by certain artificial catalysts, most of them frequently reveal slower reaction rates and lower C, and N are displayed in orange, cyan, and blue respectively). b) Proposed catalytic cycle of heme peroxidase for the oxidation of a substrate (sub) using H2O2 as oxidant.