Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803
Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803
复制标题
蓝藻集胞藻属中的硫氧还蛋白过氧化物酶。
DOI：
10.1016/s0014-5793(99)00309-9
复制
发表时间：
1999
期刊：
影响因子：
3.5
通讯作者：
A. Yokota
中科院分区：
文献类型：
--
作者：
Hiroshi Yamamoto;C. Miyake;K. Dietz;K. Tomizawa;N. Murata;A. Yokota
从集胞体中命名为sll0755的开放阅读框中推导出的氨基酸序列。PCC6803与其他生物的硫氧还蛋白过氧化物酶的氨基酸序列相似。在本研究中，我们发现在大肠杆菌中表达的重组SLL0755蛋白能够与硫氧还蛋白一起还原过氧化氢和叔丁基氢过氧化氢。Colias是电子供体。聚球藻中开放阅读框sl10755的靶向干扰。PCC6803细胞完全消除了依赖H_2O_2和依赖叔丁基氢过氧化氢的氧的光合作用和光系统II中的电子流动。这些结果表明，开放阅读框SL10755的产物是一种硫氧还蛋白过氧化物酶，其活性与集胞藻的光合作用电子传递系统相偶联。PCC 6803。
The amino acid sequence deduced from the open reading frame designated sll0755 inSynechocystissp. PCC 6803 is similar to the amino acid sequences of thioredoxin peroxidases from other organisms. In the present study, we found that a recombinant SLL0755 protein that was expressed inEscherichia coliwas able to reduce H2O2and tertiary butyl hydroperoxide with thioredoxin fromE. colias the electron donor. Targeted disruption of open reading frame sll0755 inSynechocystissp. PCC 6803 cells completely eliminated the H2O2‐dependent and tertiary butyl hydroperoxide‐dependent photosynthetic evolution of oxygen and the electron flow in photosystem II. These results indicate that the product of open reading frame sll0755 is a thioredoxin peroxidase whose activities are coupled to the photosynthetic electron transport system inSynechocystissp. PCC 6803.