Porcine polymorphonuclear leukocyte NADPH-cytochrome c reductase generates superoxide in the presence of cytochrome b559 and phospholipid.
NADPH-cytochrome c reductase and cytochrome b559 were purified from the membrane fraction of phorbol myristate acetate-stimulated porcine polymorphonuclear leukocytes. The highly purified reductase oxidized NADPH and generated superoxide when combined with partially purified cytochrome b559 in the presence of phosphatidylcholine. In the same system, but under the anaerobic condition, the reductase was found to reduce cytochrome b559.
Sakane
F
F
Kojima
H
H
Takahashi
K
K
Koyama
J
J
D000818:Animals; D003573:Cytochrome b Group / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D009504:Neutrophils / Q000201:enzymology* / Q000378:metabolism; D010084:Oxidation-Reduction; D010713:Phosphatidylcholines / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D013481:Superoxides / Q000096:biosynthesis*; D013552:Swine
D003573:Cytochrome b Group; D010713:Phosphatidylcholines; D045332:Photosystem II Protein Complex; D013481:Superoxides; C019313:cytochrome b559; D009251:NADPH-Ferrihemoprotein Reductase