SUPEROXIDE-MEDIATED RELEASE OF IRON FROM FERRITIN BY SOME FLAVOENZYMES

被引：25

作者：

BANDO, Y

AKI, K

机构：

[1] The Institute for Enzyme Research University of Tokushima Kuramoto, Tokushima

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 168卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92333-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 releases 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-methy-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. © 1990.

引用

页码：389 / 395

页数：7

共 20 条

[1] SUPEROXIDE-DEPENDENT AND SUPEROXIDE-INDEPENDENT MECHANISMS OF IRON MOBILIZATION FROM FERRITIN BY XANTHINE-OXIDASE - IMPLICATIONS FOR OXYGEN-FREE-RADICAL-INDUCED TISSUE DESTRUCTION DURING ISCHEMIA AND INFLAMMATION [J].