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首页> 外文期刊>FEBS Letters >L protein, encoded by psbL, restores normal functioning of the primary quinone acceptor, QA, in isolated D1/D2/CP47/Cytb‐559/I photosystem II reaction center core complex
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L protein, encoded by psbL, restores normal functioning of the primary quinone acceptor, QA, in isolated D1/D2/CP47/Cytb‐559/I photosystem II reaction center core complex

机译:由psbL编码的L蛋白在分离的D1 / D2 / CP47 / Cytb‐559 / I光系统II反应中心核心复合物中恢复主要醌受体QA的正常功能

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摘要

>Plastoquinone-9(PQ-9)-depleted PSII reaction center core complex, consisting of CP47/D1/D2/Cytb-55911, was isolated from spinach PSII particles. PQ-9, lipids and several proteins were extracted from the original PSII particles and separated by several steps of chromatography to be reconstituted into the isolated complex. PQ-9 reconstituted in the complex with the help of thylakoid lipids (digalactosyldiglyceride) did not function as QA by itself. However, PQ-9 simultaneously reconstituted with L protein and the thylakoid lipids successfully functioned as QA in the complex. Other proteins of PSII origin, such as CP43, H, K, nuclear encoded 4.1 and 5.0 kDa proteins, are unable to restore the QA activity in the complex.
机译:从菠菜PSII颗粒中分离出枯竭醌9(PQ-9)耗尽的PSII反应中心核心复合物,该复合物由CP47 / D1 / D2 / Cytb-55911组成。从原始PSII颗粒中提取PQ-9,脂质和几种蛋白质,并通过几个色谱步骤进行分离,以重构为分离的复合物。在类囊体脂质(地乳糖二甘油二酯)的帮助下在复合物中重构的PQ-9本身不具有Q A 的功能。然而,PQ-9同时与L蛋白重组,类囊体脂质成功地在复合物中充当Q A 。 PSII来源的其他蛋白质,例如CP43,H,K,核编码的4.1和5.0 kDa蛋白质,无法恢复复合物中的Q A 活性。

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