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- W4214754413 abstract "The enzyme NADPH oxidase in phagocytes is important in the body's defence against microbes: it produces superoxide anions (O2-, precursors to bactericidal reactive oxygen species). Electrons move from intracellular NADPH, across a chain comprising FAD (flavin adenine dinucleotide) and two haems, to reduce extracellular O2 to O2-. NADPH oxidase is electrogenic, generating electron current (I(e)) that is measurable under voltage-clamp conditions. Here we report the complete current-voltage relationship of NADPH oxidase, the first such measurement of a plasma membrane electron transporter. We find that I(e) is voltage-independent from -100 mV to >0 mV, but is steeply inhibited by further depolarization, and is abolished at about +190 mV. It was proposed that H+ efflux mediated by voltage-gated proton channels compensates I(e), because Zn2+ and Cd2+ inhibit both H+ currents and O2- production. Here we show that COS-7 cells transfected with four NADPH oxidase components, but lacking H+ channels, produce O2- in the presence of Zn2+ concentrations that inhibit O2- production in neutrophils and eosinophils. Zn2+ does not inhibit NADPH oxidase directly, but through effects on H+ channels. H+ channels optimize NADPH oxidase function by preventing membrane depolarization to inhibitory voltages. PMID: 12673252 Funding information This work was supported by: NHLBI NIH HHS, United States Grant ID: R01 HL061437" @default.
- W4214754413 created "2022-03-02" @default.
- W4214754413 creator A5063705444 @default.
- W4214754413 date "2003-04-13" @default.
- W4214754413 modified "2023-09-26" @default.
- W4214754413 title "Faculty Opinions recommendation of The voltage dependence of NADPH oxidase reveals why phagocytes need proton channels." @default.
- W4214754413 doi "https://doi.org/10.3410/f.1012959.188301" @default.
- W4214754413 hasPublicationYear "2003" @default.
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