Assembly of phagocyte NADPH oxidase: A concerted binding process?

• Published in: Biochimica et biophysica acta Vol. 1840; no. 11; pp. 3277 - 3283
• Main Authors: Karimi, Gilda, Houée Levin, Chantal, Dagher, Marie Claire, Baciou, Laura, Bizouarn, Tania
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2014; Elsevier
• Subjects: Arachidonic acid activation; binding sites; Biochemistry; Biochemistry, Molecular Biology; catalytic activity; Cell free system; Life Sciences; NAD(P)H oxidase (H2O2-forming); NADP (coenzyme); NADPH oxidase (Nox); Neutrophil; phagocytes; phagosomes; Protein translocation; proteins; superoxide anion; AA; PBS; Phox; GST; Protein translocation; Arachidonic acid activation; PMSF; Nox; ROS; ITC; MF; PX domain; FRET; NADPH oxidase (Nox); Neutrophil; Cell free system; SH3; cell-free system; human-neutrophils; respiratory burst oxidase; neutrophil; protein translocation; superoxide-production; cell free system; p67(phox); p47(phox); nadph oxidase (nox); independent activation; arachidonic acid activation; complex; phosphorylation

The phagocyte NADPH-oxidase is a multicomponent enzyme that generates superoxide anions. It comprises a membrane redox component flavocytochrome b558 and four cytosolic proteins (p67phox, p47phox, p40phox and Rac) that must assemble to produce an active system. In this work we focused on the spatio-...