England R R, Evans E H
Biochem J. 1983 Feb 15;210(2):473-6. doi: 10.1042/bj2100473.
Ca2+ has been shown to be essential for the retention of maximal O2-evolving activity in Photosystem 2 particles extracted by using dodecyldimethylamine oxide from Anacystis nidulans thylakoids. The effect cannot entirely be mimicked by using Mg2+. Ca2+ stimulates electron transport from diphenylcarbazide to 2,6-dichloroindophenol catalysed by lead-inhibited cation-free preparations, showing the presence of two cation-binding sites in these particles. Photosystem 2 preparations extracted in Ca2+-containing buffer show the presence of three polypeptides at mol. wt. 30000, 33000 and 36000, which are absent or much decreased in preparations extracted in Mg2+-containing buffer. The calmodulin antagonist chlorpromazine inhibits activity of the Photosystem 2 preparation, suggesting the presence of a Ca2+-binding protein.
已表明,对于从集胞藻6803类囊体中使用十二烷基二甲基氧化胺提取的光系统2颗粒,Ca2+对于保持最大放氧活性至关重要。使用Mg2+不能完全模拟这种效应。Ca2+刺激由铅抑制的无阳离子制剂催化的从二苯卡巴肼到2,6-二氯靛酚的电子传递,表明这些颗粒中存在两个阳离子结合位点。在含Ca2+缓冲液中提取的光系统2制剂显示存在分子量为30000、33000和36000的三种多肽,而在含Mg2+缓冲液中提取的制剂中不存在或含量大大降低。钙调蛋白拮抗剂氯丙嗪抑制光系统2制剂的活性,表明存在一种Ca2+结合蛋白。