**Abstract**

Superoxide dismutase (SOD) is a crucial enzyme required to maintain the redox potential of the cells. It plays a vital role in protecting normal cells from reactive oxygen species (ROS) produced during many intracellular pathogens infections. SOD removes excess superoxide radicals (O2−) by converting them to hydrogen peroxide (H2O2) and molecular oxygen (O2). Several superoxide dismutase enzymes have been identified based on the metal ion as a cofactor. Human SOD differs from the intracellular pathogens in having Cu/Zn and Mn as metal cofactors. However, SOD of intracellular pathogens such as *Trypanosoma, Leishmania, Plasmodium*, and *Mycobacterium* have iron (Fe) as metal cofactors. Iron Superoxide Dismutase (FeSOD) is an essential enzyme in these pathogens that neutralizes the free radical of oxygen (O<sup>−</sup> ) and prevents the formation of Peroxynitrite anion (ONOO− ), helping the pathogens escape from redox-based cytotoxic killing. Moreover, most intracellular bacteria hold MnSOD or FeSOD in their cytoplasm such as *Salmonella* and *Staphylococcus*, whereas periplasm of some pathogenic bacteria and fungi are also cofactors with Cu/Zn and identified as CuZnSOD. This chapter will review the various types SOD present in intracellular pathogens and their role in the survival of these pathogens inside their host niche.

**Keywords:** Superoxide dismutase, Intracellular Pathogen, Reactive oxygen species, Antioxidant enzyme
