Mitochondrial NADH-cytochrome b5 reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae
Mitochondrial NADH-cytochrome b5 reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae
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DOI：
10.1016/s0304-4165(01)00134-9
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发表时间：
2001-07-02
影响因子：
3
通讯作者：
Kang, SO
中科院分区：
文献类型：
--
作者：
Lee, JS;Huh, WK;Kang, SO
研究了酿酒酵母中NADH-细胞色素B（5）还原酶与依赖于NADH的D-抗坏血酸自由基还原的相关性。MCRI。已知其在S.通过将URA 3基因插入MCRI基因中，使MCRI基因被破坏。在mcr 1破坏细胞中，NADH-D-赤型抗坏血酸自由基还原酶的活性几乎消失，D-赤型抗坏血酸的细胞内水平约为同源野生型菌株的11%。在多拷贝质粒中携带MCRI的大肠杆菌细胞中，细胞内D-赤型抗坏血酸水平和NADH-D-赤型抗坏血酸自由基还原酶活性分别增加了1.7倍和2.1倍。因此，它表明，MCRI产品。线粒体NADH-细胞色素B（5）还原酶在S.啤酒。从另一方面来说。mcr 1破坏细胞对过氧化氢和甲萘醌高度敏感，而过表达MCRI使细胞对氧化应激具有更强的抵抗力。这些结果表明，线粒体NADH-细胞色素B（5）还原酶具有NADH-D-赤霉素自由基还原酶的功能，在S.啤酒。(C)2001 Elsevier Science B. V.保留所有权利。
The relevance of NADH-cytochrome b(5) reductase to the NADH-dependent reduction of D-erythroascorbyl free radical was investigated in Saccharomyces cerevisiae. MCRI. which is known to encode NADH-cytochrome b(5) reductase in S. cerevisiae, was disrupted by the insertion of URA3 gene into the gene of MCRI. In the mcr1 disruptant cells, the activity of NADH-D-erythroascorbyl free radical reductase almost disappeared and the intracellular level of D-erythroascorbic acid was about 11% of that of the congenic wild-type strain. In the transformant cells carrying MCRI in multicopy plasmid, the intracellular level of D-erythroascorbic acid and the activity of NADH-D-erythroascorbyl free radical reductase increased up to 1.7-fold and 2.1-fold, respectively. Therefore, it indicated that the,MCRI product. mitochondrial NADH-cytochrome b(5) reductase, plays a key role in the NADH-dependent reduction of D-erythroascorbyl free radical in S. cerevisiae. On the other hand. the mcr1 disruptant cells were hypersensitive to hydrogen peroxide and menadione, and overexpression of MCRI made the cells more resistant against oxidative stress. These results suggested that the mitochondrial NADH-cytochrome b(5) reductase functions as NADH-D-erythroascorbyl free radical reductase and plays an important role in the response to oxidative damage in S. cerevisiae. (C) 2001 Elsevier Science B.V. All rights reserved.