NADPH-dependent electron transport chain in microsomes and lipid peroxidation catalyzed by metal ions

Acta Biol Med Ger. 1979;38(2-3):435-42.

Abstract

Like iron ions copper ions are also able to stimulate the NADPH-dependent lipid peroxidation in rat liver microsomes. This effect is strongly dependent on the concentration of Cu2+ added. Initial concentrations of Cu2+ above 50 microM completely inhibit the formation of malonaldehyde. The activator and inhibitor functions may be interpreted by a simultaneous participation of Cu+ ions formed in the chain branching and termination reaction of the free radical lipid peroxidation process. Inhibition studies with pCMB and the His-reagent diethyl pyrocarbonate indicate an essential role of cysteine and histidine residues in the Cu+-NADPH-dependent lipid peroxidation process.

MeSH terms

  • Animals
  • Chloromercuribenzoates / pharmacology
  • Copper / pharmacology
  • Cytochrome P-450 Enzyme System / metabolism*
  • Iron / pharmacology
  • Kinetics
  • Lipid Peroxides / metabolism*
  • Male
  • Malondialdehyde
  • Microsomes, Liver / metabolism*
  • NADP / metabolism*
  • Rats

Substances

  • Chloromercuribenzoates
  • Lipid Peroxides
  • Malondialdehyde
  • NADP
  • Copper
  • Cytochrome P-450 Enzyme System
  • Iron