Reconstitution of oxygen evolution in high salt washed photosystem II particles.
Reconstitution of oxygen evolution in high salt washed photosystem II particles.
复制标题
高盐洗涤光系统 II 颗粒中氧气释放的重建。
DOI：
10.1016/0006-291x(83)91061-6
复制
发表时间：
1983
期刊：
影响因子：
--
通讯作者：
H. Akerlund
中科院分区：
文献类型：
--
作者：
U. Ljungberg;C. Jansson;B. Andersson;H. Akerlund
光系统II类囊体颗粒具有高速率的氧释放，被证明有一个非常简单的多肽组成。在用250 mM NaCl洗涤这些颗粒时，伴随着23和16 kDa的两种多肽的释放，氧释放被抑制高达80%。在低离子强度下将纯的23 kDa蛋白质重新添加到耗尽的类囊体中，重建了超过一半的失去的活性。单独使用16 kDa蛋白或与甘油组合使用16 kDa蛋白均未获得刺激。这些结果进一步有力地证明了23 kDa蛋白质是氧释放复合物的重要组成部分。光系统II粒子的简单多肽模式的光系统II粒子在这个复杂的其他蛋白质的可能参与进行了讨论。
Photosystem II thylakoid particles possessing high rates of oxygen evolution, were shown to have a very simple polypeptide composition. Upon washing of these particles with 250 mM NaCl the oxygen evolution was inhibited up to 80% concomitant with a release of two polypeptides of 23 and 16 kDa. Readdition of the pure 23 kDa protein to the depleted thylakoids under low ionic strength reconstituted more than half of the lost activity. No stimulation was obtained with the 16 kDa protein alone or in combination with glycerol. The results give further strong evidence that the 23 kDa protein is an essential component in the oxygen evolving complex. The possible involvement of other proteins in this complex is discussed in light of the demonstrated simple polypeptide pattern of the photosystem II particles.