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Electron currents generated by the human phagocyte NADPH oxidase

Author

Listed:
  • Jacques Schrenzel

    (University Hospital
    Mayo Clinic)

  • Lena Serrander

    (University Hospital)

  • Botond Bánfi

    (University Hospital
    Semmelweis Medical University)

  • Oliver Nüße

    (University Hospital)

  • Reyhaneh Fouyouzi

    (University Hospital)

  • Daniel P. Lew

    (University Hospital)

  • Nicolas Demaurex

    (University Medical Center)

  • Karl-Heinz Krause

    (University Hospital)

Abstract

Electron transport across biological membranes is a well-known feature of bacteria, mitochondria and chloroplasts, where it provides motive forces for vectorial transport processes1. In contrast, electron transport is generally not found in the plasma membrane of eukaryotic cells, possibly because it would interfere with electric processes at the plasma membrane. An exception is provided by the phagocyte NADPH oxidase, which generates superoxide ( ) through electron transfer from cytosolic NADPH to extracellular oxygen2,3,4,5. The enzyme is essential for host defence, and patients with chronic granulomatous disease, who lack the functional enzyme, suffer from severe infections6,7. It has been suggested that electron transfer by the NADPH oxidase might be electrogenic8. Here we demonstrate, using the whole-cell patch-clamp technique, the generation of electron currents by the NADPH oxidase in human eosinophil granulocytes. The currents were absent in granulocytes of sufferers of chronic granulomatous disease and under conditions of low oxygen. Generation of electron currents across the plasma membrane of eukaryotic cells has not been observed previously and might be — independently of the generation of superoxide — a physiologically relevant function of the phagocyte NADPH oxidase.

Suggested Citation

  • Jacques Schrenzel & Lena Serrander & Botond Bánfi & Oliver Nüße & Reyhaneh Fouyouzi & Daniel P. Lew & Nicolas Demaurex & Karl-Heinz Krause, 1998. "Electron currents generated by the human phagocyte NADPH oxidase," Nature, Nature, vol. 392(6677), pages 734-737, April.
  • Handle: RePEc:nat:nature:v:392:y:1998:i:6677:d:10.1038_33725
    DOI: 10.1038/33725
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