期刊
MICROBIOLOGY-SGM
卷 155, 期 -, 页码 1840-1846出版社
SOC GENERAL MICROBIOLOGY
DOI: 10.1099/mic.0.026260-0
关键词
-
类别
资金
- Fondecyt and Dicyt-USACH [1060022]
- Conicyt and Dicyt-USACH, Chile
- MECESUP, Chile
The tellurium oxyanion tellurite is toxic for most organisms and it seems to alter a number of intracellular targets. In this work the toxic effects of tellurite upon Escherichia coli [4Fe-4S] cluster-containing dehydratases was studied. Reactive oxygen species (ROS)-sensitive fumarase A (FumA) and aconitase B (AcnB) as well as ROS-resistant fumarase C (FumC) and aconitase A (AcnA) were assayed in cell-free extracts from tellurite-exposed cells in both the presence and absence of oxygen. While over 90% of FumA and AcnB activities were lost in the presence of oxygen, no enzyme inactivation was observed in anaerobiosis. This result was not dependent upon protein biosynthesis, as determined using translation-arrested cells. Enzyme activity of purified FumA and AcnB was inhibited when exposed to an in vitro superoxide-generating, tellurite-reducing system (ITRS). No inhibitory effect was observed when tellurite was omitted from the ITRS. In vivo and in vitro reconstitution experiments with tellurite-damaged FumA and AcnB suggested that tellurite effects involve [Fe-S] cluster disabling. In fact, after exposing FumA to ITRS, released ferrous ion from the enzyme was demonstrated by spectroscopic analysis using the specific Fe2+ chelator 2,2'-bipyridyl. Subsequent spectroscopic paramagnetic resonance analysis of FumA exposed to ITRS showed the characteristic signal of an oxidatively inactivated [3Fe-4S](+) cluster. These results suggest that tellurite inactivates enzymes of this kind via a superoxide-dependent disabling of their [4Fe-4S] catalytic clusters.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据