Yamamoto H, Miyake C, Dietz K J, Tomizawa K, Murata N, Yokota A
Plant Molecular Physiology Laboratory, Research Institute of Innovative Technology for the Earth, Kizu, Kyoto, Japan.
FEBS Lett. 1999 Mar 26;447(2-3):269-73. doi: 10.1016/s0014-5793(99)00309-9.
The amino acid sequence deduced from the open reading frame designated sll0755 in Synechocystis sp. 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 in Escherichia coli was able to reduce H2O2 and tertiary butyl hydroperoxide with thioredoxin from E. coli as the electron donor. Targeted disruption of open reading frame sll0755 in Synechocystis sp. 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 in Synechocystis sp. PCC 6803.
从集胞藻PCC 6803中指定为sll0755的开放阅读框推导出来的氨基酸序列，与其他生物体中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蛋白能够以大肠杆菌的硫氧还蛋白作为电子供体来还原过氧化氢和叔丁基过氧化氢。对集胞藻PCC 6803细胞中的开放阅读框sll0755进行靶向破坏，完全消除了依赖过氧化氢和叔丁基过氧化氢的光合放氧以及光系统II中的电子流动。这些结果表明，开放阅读框sll0755的产物是一种硫氧还蛋白过氧化物酶，其活性与集胞藻PCC 6803中的光合电子传递系统相关联。
