F‐695 emission from the purified photosystem II chlorophyll a‐protein complex

F‐695 emission from the purified photosystem II chlorophyll a‐protein complex
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纯化光系统 II 叶绿素 a 蛋白复合物的 F-695 发射

DOI:
10.1016/0014-5793(80)80021-4
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发表时间:
1980
期刊:
影响因子:
3.5
通讯作者:
K. Satoh
K. Satoh
中科院分区:
生物学3区
文献类型:
--
作者:
K. Satoh

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早期的分离实验[L-4]以及荧光激发光谱[5,6]和荧光诱导[7,8]的分析支持了F-685和F-695在光合作用中属于光系统II(PSII),而F-735属于光系统I(PSI)的结论。然而,F-695带被认为是来自PSI1反应中心[9]天线的荧光,它既没有出现在光收获的纯化制剂中([131,但见[23]),也没有出现在纯化的反应中心复合体中[PSII的LO-151]。这种差异首先由假设[13]解释,即F-685和F-695是由于PSII的捕光和反应中心复合体,但在洗涤剂增溶的制剂中,峰位置分别蓝移到681和685 nm。然而,这一假说受到以下事实的挑战:在缺乏捕光能力的叶绿素a/b蛋白[161]的突变大麦的叶绿体光谱上观察到685 nm附近的显著发射带[161],以及纯化的PSI1叶绿素a蛋白复合体(包括PSI1[11,13,171]的叶绿素a蛋白)的F-685发射不再显示叶绿体F-695发射的特征温度依赖性。为了从类囊体膜分离色素蛋白复合体中获得更多关于F695命运的信息,我们用一种灵敏的方法对F-695带进行了检测在杂色试剂存在下的邻菲咯啉[181.结果表明,纯化的PSI1叶绿素a-蛋白复合体含有F-685和F685两种荧光成分
Early fractionation experiments [l-4] as well as the analysis of fluorescence excitation spectra [5, 6] and of fluorescence inductions [7, 8] supported the conclusion that F-685 and F-695 belong to photosystern II (PSII) while F-735 belongs to photosystem I (PSI) in photosynthesis. However, the F-695 band, which has been postulated as fluorescence originating from the antenna of the PSI1 reaction center [9], appeared neither in the purified preparations of lightharvesting ([131, but see [23]) nor in the purified reaction center complex [lo-151 of PSII. This discrepancy was first explained by the hypothesis [13] that F-685 and F-695 are due to the light-harvesting and the reaction center complex of PSII, but that the peak positions are blue-shifted in the detergent-solubilized preparations to 681 and 685 nm, respectively. The hypothesis, however, is challenged by the facts that a prominent emission band near 685 nm is observed on the spectrum of chloroplasts from mutant barley lacking the light-harvesting chlorophyll a/b-protein [161 and that the F-685 emission of the purified PSI1 chlorophyll a-protein complex (the chlorophyll a-protein comprising the reaction center of PSI1 [11, 13, 171) no longer shows the characteristic temperature dependence of chloroplast F-695 emission.In order to gain more information about the fate of F695 in isolation of pigment-protein complexes from the thylakoid membranes, an analysis was carried out to detect F-695 band by a sensitive method which uses 1, lO-phenanthroline in the presence of chaotropic reagents [181. The results clearly indicated that the purified PSI1 chlorophyll a-protein complex contains two fluorescent components, F-685 and