Affordable Access

Superoxide-mediated release of iron from ferritin by some flavoenzymes.

Authors
  • Bando, Y
  • Aki, K
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Apr 30, 1990
Volume
168
Issue
2
Pages
389–395
Identifiers
PMID: 2159290
Source
Medline
License
Unknown

Abstract

NADH-lipoamide dehydrogenase mobilized iron from ferritin under aerobic conditions. Superoxide dismutase strongly inhibited this mobilization, indicating that the superoxide radical is generated by the enzymatic reaction and release iron from ferritin. Addition of lipoamide as an electron acceptor to NADH-lipoamide dehydrogenase increased the release of iron from ferritin and this release was partially inhibited by superoxide dismutase. Similarly, addition of menadione (2-methyl-1, 4-naphthoquinone) as an electron acceptor to xanthine-xanthine oxidase promoted the release of iron from ferritin and this release was strongly inhibited by superoxide dismutase. These results suggest that dihydrolipoamide and semiquinone of menadione can react with oxygen to form the superoxide radical that mediates release of iron from ferritin.

Report this publication

Statistics

Seen <100 times