Ascorbate-mediated electron transfer in protein thiol oxidation in the endoplasmic reticulum

被引：32

作者：

Csala, M

Braun, L

Mile, V

Kardon, T

Szarka, A

Kupcsulik, P

Mandl, J

Bánhegyi, G

机构：

[1] Semmelweis Univ Med, Dept Med Chem, H-1444 Budapest, Hungary

[2] Semmelweis Univ Med, Dept Surg 1, H-1444 Budapest, Hungary

来源：

FEBS LETTERS | 1999年 / 460卷 / 03期

关键词：

ascorbate; dehydroascorbate; protein thiol; hydrogen peroxide; gulonolactone oxidase; endoplasmic reticulum;

D O I：

10.1016/S0014-5793(99)01412-X

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：

Addition of, or gulonolactone oxidase-dependent in situ generation of, ascorbate provoked the oxidation of protein thiols, which was accompanied by ascorbate consumption in liver microsomal vesicles. The maximal rate of protein thiol oxidation was similar upon gulonolactone, ascorbate or dehydroascorbate addition. Cytochrome P450 inhibitors (econazole, proadifen, quercetin) decreased ascorbate consumption and the gulonolactone or ascorbate-stimulated thiol oxidation, The results demonstrate that the ascorbate/dehydroascorbate redox couple plays an important role in electron transfer from protein thiols to oxygen in the hepatic endoplasmic reticulum, even in gulonolactone oxidase deficient species. (C) 1999 Federation of European Biochemical Societies.

引用

页码：539 / 543

页数：5

共 37 条

[1] Oxidative protein folding is driven by the electron transport system [J].