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NADPH oxidase complex subunits are integral components of the multisubunit NADPH oxidase enzyme complex, which catalyzes the generation of reactive oxygen species (ROS) such as superoxide by transferring electrons from NADPH to oxygen[1][2][6]. The best-studied complex, in phagocytes, consists of a membrane-bound heterodimeric core (gp91^phox^, also called NOX2, and p22^phox^) and cytosolic subunits (p47^phox^, p67^phox^, p40^phox^, and Rac GTPase)[1][2][6]. Upon activation (e.g., during phagocytosis), cytosolic subunits translocate to the membrane, assemble with the core, and activate superoxide generation critical for microbial killing and signal transduction[2][4][5]. Defects in these subunits underlie chronic granulomatous disease[6]. NOX subunit homologs exist in many tissues, serving roles in host defense, inflammation, vascular physiology, and cell signaling[1][4][5].
Inhibition of ROS production (inhibitors block electron transfer, inhibiting formation of superoxide and downstream ROS); Interference with NADPH/FAD/heme electron transfer (small molecules may block specific redox cofactors)
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