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• W2051201020 endingPage "7480" @default.
• W2051201020 startingPage "7474" @default.
• W2051201020 abstract "The leukocyte NADPH oxidase of neutrophils is a membrane-bound enzyme that catalyzes the production of O2- from oxygen using NADPH as electron donor. Dormant in resting neutrophils, the enzyme acquires catalytic activity when the cells are exposed to appropriate stimuli. During activation, the cytosolic oxidase components p47phox and p67phox migrate to the plasma membrane, where they associate with cytochrome b558, a membrane-bound flavohemoprotein, to assemble the active oxidase. An essential element of the activation process is the phosphorylation of p47phox, an event that accompanies oxidase activation in whole cells and can activate the oxidase in a cell-free system. We show here that the phosphorylation of p47phox leads to a substantial decrease in the reactivity of cysteine C378 toward N-ethylmaleimide, indicating the occurrence of a conformational change involving the C-terminal region of p47phox. A similar conformational change occurs when p47phox is exposed to arachidonate, one of a number of anionic detergents that activate the oxidase in the cell-free system. We propose that this change in conformation results in the appearance of a binding site through which p47phox interacts with cytochrome b558 during the activation process." @default.
• W2051201020 created "2016-06-24" @default.
• W2051201020 creator A5039679762 @default.
• W2051201020 creator A5090237506 @default.
• W2051201020 date "1997-06-01" @default.
• W2051201020 modified "2023-09-26" @default.
• W2051201020 title "Activation of the Leukocyte NADPH Oxidase Subunit p47<i>^phox</i> by Protein Kinase C. A Phosphorylation-Dependent Change in the Conformation of the C-Terminal End of p47<i>^phox</i>" @default.
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• W2051201020 doi "https://doi.org/10.1021/bi9700936" @default.
• W2051201020 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9200696" @default.
• W2051201020 hasPublicationYear "1997" @default.
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