Degradation and covalent cross-linking of glutathione reductase by hemin

Life Sci. 1985 Jun 3;36(22):2153-61. doi: 10.1016/0024-3205(85)90312-1.

Abstract

Hemin (ferriprotoporphyrin IX-chloride) can mediate the covalent cross-linking and degradation of yeast glutathione reductase. This reaction requires both NADPH and oxygen suggesting the involvement of a reduced oxygen species in the cross-linking and degradation process. During the course of the reaction the enzymatic activity of glutathione reductase is rapidly destroyed. Implications of these findings for a regulatory role of hemin in cell biology are discussed.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Glutathione Reductase*
  • Heme / analogs & derivatives*
  • Hemin / pharmacology*
  • NADP / pharmacology
  • Oxygen / pharmacology
  • Yeasts / enzymology

Substances

  • Heme
  • NADP
  • Hemin
  • Glutathione Reductase
  • Oxygen