Superoxide dismutase and other antioxidant enzymes (SOD)

Superoxide dismutase (SOD) and other antioxidant enzymes, including catalase and glutathione peroxidase, represent the primary enzymatic defense network against oxidative damage in aerobic organisms. These enzymes work synergistically to neutralize reactive oxygen species (ROS) by converting superoxide radicals into hydrogen peroxide and subsequently into water and molecular oxygen, thereby maintaining cellular redox homeostasis [1, 2]. Dysregulation or genetic mutations in these enzymes, most notably SOD1, are directly implicated in the pathogenesis of neurodegenerative conditions such as amyotrophic lateral sclerosis (ALS) and contribute to the progression of cardiovascular diseases and chronic inflammation [1, 5]. In therapeutic contexts, these enzymes or their synthetic mimics are utilized to mitigate tissue damage caused by excessive ROS production during events like ischemia-reperfusion or inflammatory flares [3, 6]. Despite their significant therapeutic potential, clinical application is often hampered by challenges related to protein stability, short half-lives, and the risk of disrupting beneficial ROS-mediated signaling pathways [2, 4]. Consequently, current research focuses on developing stable enzyme mimics and delivery systems to enhance the efficacy of antioxidant therapy [6]. [1] UniProt Consortium (P00441); [2] Ighodaro & Akinloye (2018) Alexandria Journal of Medicine; [3] PubChem (CID 16212401); [4] Azadmanesh & Borgstahl (2018) Antioxidants; [5] Zelko et al. (2002) Free Radical Biology and Medicine; [6] Batinic-Haberle et al. (2010) Antioxidants & Redox Signaling.

Other names

SODCatalaseGlutathione peroxidaseGPxAntioxidant defense systemOxidoreductasesReactive oxygen species scavengers

Catalytic disproportionation of superoxide radicals into oxygen and hydrogen peroxide; reduction of hydrogen peroxide and hydroperoxides to water and alcohols; scavenging of free radicals to prevent lipid peroxidation and macromolecular damage.