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Free radical scavenging enzymes are a critical group of proteins responsible for maintaining cellular redox homeostasis by neutralizing reactive oxygen species (ROS) and reactive nitrogen species (RNS) (StatPearls, 2023). This group primarily includes superoxide dismutase (SOD), which converts superoxide radicals into hydrogen peroxide, and catalase, which decomposes hydrogen peroxide into water and oxygen (UniProt, 2024). Additionally, the glutathione peroxidase (GPx) and thioredoxin systems reduce various peroxides using thiol-based cofactors to prevent cellular damage (PubMed, PMID: 30264648). Under physiological conditions, these enzymes protect DNA, proteins, and lipids from oxidative modification, a process essential for preventing premature aging and chronic disease (NIH, 2022). Dysregulation or overwhelming of these enzymatic defenses leads to oxidative stress, which is a central driver in neurodegenerative diseases, cardiovascular disorders, and inflammatory conditions (PubMed, PMID: 28851713). Pharmacological strategies involve the use of small-molecule mimetics, such as the GPx mimic Ebselen, or the induction of endogenous enzyme production through Nrf2 activators like Bardoxolone methyl (PubChem, 2024). However, therapeutic targeting is complex because ROS also function as vital signaling molecules in immune defense and cell proliferation (Nature Reviews Drug Discovery, 2020).
Catalytic neutralization of reactive oxygen species (ROS) into non-toxic molecules like water and oxygen, or pharmacological induction of endogenous enzyme expression via the Nrf2/ARE signaling pathway.
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