...
首页> 外文期刊>Plant signaling & behavior >Changes in thylakoid membrane thickness associated with the reorganization of photosystem II light harvesting complexes during photoprotective energy dissipation.
【24h】

Changes in thylakoid membrane thickness associated with the reorganization of photosystem II light harvesting complexes during photoprotective energy dissipation.

机译:在光防护能量耗散过程中类囊体膜厚度的变化与光系统II集光复合物的重组有关。

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

Using freeze-fracture electron microscopy we have recently shown that non-photochemical quenching (NPQ), a mechanism of photoprotective energy dissipation in higher plant chloroplasts, involves a reorganization of the pigment-protein complexes within the stacked grana thylakoids. Photosystem II light harvesting complexes (LHCII) are reorganized in response to the amplitude of the light driven transmembrane proton gradient ([Greek capital Delta]pH) leading to their dissociation from photosystem II reaction centers and their aggregation within the membrane1. This reorganization of the PSII-LHCII macrostructure was found to be enhanced by the formation of zeaxanthin and was associated with changes in the mobility of the pigment-protein complexes therein1. We suspected that the structural changes we observed were linked to the [Greek capital Delta]pH-induced changes in thylakoid membrane thickness that were first observed by Murikami and Packer. Here using thin-section electron microscopy we show that the changes in thylakoid membrane thickness do not correlate with [Greek capital Delta]pH per se but rather the amplitude of NPQ and is thus affected by the de-epoxidation of the LHCII bound xanthophyll violaxanthin to zeaxanthin. We thus suggest that the change in thylakoid membrane thickness occurring during NPQ reflects the conformational change within LHCII proteins brought about by their protonation and aggregation within the membrane
机译:最近,我们使用冷冻断裂电子显微镜显示,非光化学淬灭(NPQ)是高等植物叶绿体中光保护能量消散的一种机制,涉及到堆积的类花生类生物体中色素-蛋白质复合物的重组。光系统II集光复合物(LHCII)响应于光驱动的跨膜质子梯度(希腊资本ΔpH)的幅度而重组,从而导致它们从光系统II反应中心解离并在膜内聚集。玉米黄质的形成增强了PSII-LHCII宏观结构的这种重组,并与其中的色素-蛋白质复合物的迁移率变化有关。我们怀疑我们观察到的结构变化与希腊化合物ΔpH引起的类囊体膜厚度变化有关,这是由Murikami和Packer首先观察到的。在此使用薄层电子显微镜,我们显示类囊体膜厚度的变化本身与希腊资本ΔpH本身不相关,而是与NPQ的幅度相关,因此受LHCII结合的叶黄素紫黄质素的脱环氧化作用的影响。玉米黄质。因此,我们建议NPQ期间类囊体膜厚度的变化反映了LHCII蛋白内的构象变化,这是由它们在膜内的质子化和聚集引起的

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号