Oxygen is required for the L-cysteine-mediated decomposition of protein-bound dinitrosyl-iron complexes.
Oxygen is required for the L-cysteine-mediated decomposition of protein-bound dinitrosyl-iron complexes.
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DOI：
10.1016/j.freeradbiomed.2010.04.012
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发表时间：
2010-07-15
影响因子：
7.4
通讯作者：
Ding, Huangen
中科院分区：
文献类型：
--
作者：
Yang, Juanjuan;Duan, Xuewu;Landry, Aaron P.;Ding, Huangen
越来越多的证据表明，铁硫蛋白是NO（一氧化氮）的主要靶点。大肠杆菌细胞暴露于NO容易将铁硫蛋白转化为蛋白质结合的DNIC（二亚硝酰铁复合物）。虽然蛋白结合的DNIC在体外有氧或厌氧条件下是稳定的，但它们在有氧生长的E.大肠杆菌细胞甚至没有新的蛋白质合成。NO修饰的铁硫蛋白的细胞修复机制在很大程度上仍然难以捉摸。在这里，我们报告说，不像有氧生长E。coli细胞，饥饿的E.大肠杆菌细胞不能重新激活NO修饰的铁硫蛋白。值得注意的是，加入L-半胱氨酸，而不是其他相关的生物硫醇，导致饥饿的E.大肠杆菌细胞和在有氧条件下的细胞提取物中。然而，L-半胱氨酸对饥饿的E.大肠杆菌细胞和体外厌氧条件下，表明氧是必需的L-半胱氨酸介导的蛋白结合的DNIC的分解。另外的研究表明，L-半胱氨酸能够将DNIC与蛋白质结合的DNIC交换以形成L-半胱氨酸结合的DNIC，其被氧气快速破坏，导致蛋白质结合的DNIC在有氧条件下最终分解。
Increasing evidence suggests that iron-sulfur proteins are the primary targets of NO (nitric oxide). Exposure of Escherichia coli cells to NO readily converts iron-sulfur proteins to the protein-bound DNICs (dinitrosyl iron complexes). While the protein-bound DNICs are stable in vitro under aerobic or anaerobic conditions, they are efficiently repaired in aerobically growing E. coli cells even without new protein synthesis. The cellular repair mechanism for the NO-modified iron-sulfur proteins remains largely elusive. Here we report that unlike aerobically growing E. coli cells, the starved E. coli cells fail to re-activate the NO-modified iron-sulfur proteins. Significantly, addition of L-cysteine, but not other related biological thiols, results in decomposition of the protein-bound DNICs in the starved E. coli cells and in the cell extracts under aerobic conditions. However, L-cysteine has little or no effect on the protein-bound DNICs in the starved E. coli cells and in vitro under anaerobic conditions, suggesting that oxygen is required for the L-cysteine-mediated decomposition of the protein-bound DNICs. Additional studies reveal that L-cysteine is able to exchange the DNIC with the protein-bound DNICs to form the L-cysteine-bound DNIC which is rapidly disrupted by oxygen, resulting in eventual decomposition of the protein-bound DNICs under aerobic conditions.
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影响因子：
2.9
作者：
GREEN, LC;WAGNER, DA;TANNENBAUM, SR
通讯作者：
TANNENBAUM, SR
DOI：
10.1073/pnas.0306706101
发表时间：
2004-03-23
影响因子：
11.1
作者：
Bryan, NS;Rassaf, T;Feelisch, M
通讯作者：
Feelisch, M
影响因子：
4.8
作者：
Kennedy, MC;Antholine, WE;Beinert, H
通讯作者：
Beinert, H
影响因子：
2.9
作者：
COWART, RE;SINGLETON, FL;HIND, JS
通讯作者：
HIND, JS
影响因子：
4.8
作者：
Justino, Marta C.;Almeida, Claudia C.;Saraiva, Ligia M.
通讯作者：
Saraiva, Ligia M.