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Ascorbate-dependent electron transfer across the human erythrocyte membrane.

J M May1, Z C Qu

  • 1Departments of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232-6303, USA. james.may@mcmail.vanderbilt.edu

Biochimica Et Biophysica Acta
|November 16, 1999
PubMed
Summary

Human red blood cells reduce ferricyanide using an unknown enzyme, limited by intracellular ascorbic acid recycling. This enzyme is a transmembrane protein with sulfhydryl groups on both sides.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Membrane Transport

Background:

  • Extracellular ferricyanide reduction by intact cells indicates a trans-plasma membrane oxidoreductase activity.
  • This activity in human erythrocytes is primarily dependent on intracellular ascorbic acid recycling.

Purpose of the Study:

  • To identify the enzyme responsible for trans-plasma membrane ferricyanide reduction in human erythrocytes.
  • To elucidate the role of ascorbic acid and the enzyme's structure in this process.

Main Methods:

  • Utilized intact erythrocytes and resealed/open erythrocyte ghosts.
  • Employed p-chloromercuribenzene sulfonic acid to probe sulfhydryl group involvement.
  • Used proteases (trypsin, pronase) to investigate enzyme accessibility.

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Main Results:

  • Ascorbate-dependent ferricyanide reduction was limited by intracellular ascorbic acid recycling.
  • Sulfhydryl modification on intact cells affected subsequent ghost activity, indicating membrane association.
  • Proteolytic digestion of resealed ghosts increased ascorbate-dependent activity, suggesting enzyme location and accessibility.

Conclusions:

  • The trans-membrane ferricyanide oxidoreductase is limited by intracellular ascorbate recycling.
  • This enzyme is distinct from the NADH-dependent cytochrome b(5) reductase system.
  • It is a transmembrane protein with accessible sulfhydryl groups on both cytoplasmic and extracellular faces.