Department of Chemistry, University of Crete, Iraklion, Crete, Greece.
Photosynth Res. 1991 Sep;29(3):149-55. doi: 10.1007/BF00036218.
Selective extraction-reconstitution experiments with the extrinsic Photosystem II polypeptides (33 kDa, 23 kDa and 17 kDa) have demonstrated that the manganese complex and the 33 kDa polypeptide are both necessary structural elements for the tight binding of the water soluble 17 and 23 kDa species. When the manganese complex is intact the 33 kDa protein interacts strongly with the rest of the photosynthetic complex. Destruction of the Mn-complex has two dramatic effects: i) The binding of the 33 kDa polypeptide is weaker, since it can be removed by exposure of the PS II system to 2 M NaCl, and ii) the 17 and 23 kDa species do not rebind to Mn-depleted Photosystem II membranes that retain the 33 kDa protein.
采用外源 PS II 多肽（33kDa、23kDa 和 17kDa）的选择萃取-再结合实验证明，锰复合物和 33kDa 多肽都是牢固结合可溶于水的 17kDa 和 23kDa 两种物质所必需的结构要素。当锰复合物完整时，33kDa 蛋白与光合作用复合物的其余部分强烈相互作用。锰复合物的破坏有两个显著的影响：i）33kDa 多肽的结合较弱，因为它可以通过将 PS II 系统暴露于 2M NaCl 中而被去除；ii）17kDa 和 23kDa 物质不会再结合到保留 33kDa 蛋白的锰耗竭 PS II 膜上。
