Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase

被引：25

作者：

Riebe, Oliver ^{[1
]}

Fischer, Ralf-Joerg ^{[1
]}

Bahl, Hubert ^{[1
]}

机构：

[1] Univ Rostock, Inst Biol Sci, Div Microbiol, D-18051 Rostock, Germany

来源：

FEBS LETTERS | 2007年 / 581卷 / 29期

关键词：

oxidative stress; superoxide reductase; anaerobic bacteria; Clostridium;

D O I：

10.1016/j.febslet.2007.11.008

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：

Desulfoferrodoxin (cac2450) of Clostridium acetobutylicum was purified after overexpression in E. coli. In an in vitro assay the enzyme exhibited superoxide reductase activity with rubredoxin (cac2778) of C. acetobutylicum as the proximal electron donor. Rubredoxin was reduced by ferredoxin: NADP+ reductase from spinach and NADPH. The superoxide anions, generated from dissolved oxygen using Xanthine and Xanthine oxidase, were reduced to hydrogen peroxide. Thus, we assume that desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：5605 / 5610

页数：6

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