Assembly of the phagocyte NADPH oxidase complex: chimeric constructs derived from the cytosolic components as tools for exploring structure-function relationships.

@article{Mizrahi2006AssemblyOT,
  title={Assembly of the phagocyte NADPH oxidase complex: chimeric constructs derived from the cytosolic components as tools for exploring structure-function relationships.},
  author={Ariel Bezaleli Mizrahi and Yevgeny Berdichevsky and Yelena Ugolev and Shahar Molshanski-Mor and Yael Nakash and Iris Dahan and Nathalie Alloul and Yara Gorzalczany and Rive Sarfstein and Miriam Hirshberg and Edgar Pick},
  journal={Journal of leukocyte biology},
  year={2006},
  volume={79 5},
  pages={881-95}
}
Phagocytes generate superoxide (O2*-) by an enzyme complex known as reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase. Its catalytic component, responsible for the NADPH-driven reduction of oxygen to O2*-, is flavocytochrome b559, located in the membrane and consisting of gp91phox and p22phox subunits. NADPH oxidase activation is initiated by the translocation to the membrane of the cytosolic components p47phox, p67phox, and the GTPase Rac. Cytochrome b559 is converted to an… CONTINUE READING

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