Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli

被引：75

作者：

Liochev, SI

Hausladen, A

Fridovich, I ^{[1
]}

机构：

[1] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA

[2] Duke Univ, Med Ctr, Howard Hughes Med Res Inst, Durham, NC 27710 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 07期

关键词：

D O I：

10.1073/pnas.96.7.3537

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Nitroreductase A catalyzes the divalent reduction of nitro compounds, quinones, and dyes by NADPH. In this paper, nitroreductase A is induced in Escherichia coli by exposure to paraquat in a manner that depends on the expression of soxR. Nitroreductase activity was only slightly induced by paraquat in a strain bearing a mutational defect in the gene encoding nitroreductase A, but it was approximate to 3-fold induced in the parental strain. Nitroreductase A thus appears to be a member of the soxRS regulon and probably contributes to the defenses against oxidative stress by minimizing the redox cycling attendant upon the univalent reduction of nitro compounds, quinones, and dyes.

引用

页码：3537 / 3539

页数：3

共 21 条

[1]

ARIZA RR, 1995, J BACTERIOL, V177, P1651

[2] DIHYDROXY-ACID DEHYDRATASE, A [4FE-4S] CLUSTER-CONTAINING ENZYME IN ESCHERICHIA-COLI - EFFECTS OF INTRACELLULAR SUPEROXIDE-DISMUTASE ON ITS INACTIVATION BY OXIDANT STRESS [J].