Reactive oxygen species-related enzymes and redox signaling (ROS/Redox Signaling)

Reactive oxygen species (ROS)-related enzymes and redox signaling encompass a diverse group of proteins that generate, scavenge, or respond to oxygen-derived free radicals and non-radical species. Key enzymes include NADPH oxidases (NOX), which produce ROS for signaling and defense, and antioxidant enzymes like superoxide dismutase (SOD), catalase, and glutathione peroxidase (GPx), which maintain redox homeostasis [1][2]. Redox signaling involves the reversible oxidative modification of specific protein residues, such as cysteine thiols, which acts as a molecular switch to regulate various cellular processes including proliferation, differentiation, and apoptosis [3]. Dysregulation of this system leads to oxidative stress, a state characterized by an imbalance between ROS production and antioxidant defenses, contributing to the pathogenesis of cancer, neurodegeneration, and cardiovascular diseases [4]. Therapeutic strategies targeting this system include the use of ROS scavengers, inhibitors of ROS-generating enzymes, and activators of the Nrf2-Keap1 pathway to enhance endogenous antioxidant capacity [5]. However, achieving therapeutic precision remains challenging due to the dual role of ROS as both essential signaling molecules and damaging agents [6].

Other names

Oxidative stress enzymesRedox-regulating enzymesAntioxidant enzymesROS signaling pathwayRedoxome

The mechanisms include direct scavenging of reactive oxygen species, inhibition of ROS-producing enzymes like NADPH oxidase, activation of the Nrf2-Keap1 pathway to induce endogenous antioxidant gene expression, and the use of synthetic mimics of enzymes such as superoxide dismutase and glutathione peroxidase [2][5].