Suppr超能文献

完整细胞和含叶绿素 d 的蓝藻鱼腥藻藻蓝蛋白天线中的激发能转移。

Excitation energy transfer in intact cells and in the phycobiliprotein antennae of the chlorophyll d containing cyanobacterium Acaryochloris marina.

机构信息

Institute of Optics and Atomic Physics, Technische Universität Berlin, Strasse des 17. Juni 135, Berlin, Germany.

出版信息

J Plant Physiol. 2011 Aug 15;168(12):1473-87. doi: 10.1016/j.jplph.2011.02.002. Epub 2011 Mar 10.

Abstract

The cyanobacterium Acaryochloris marina is unique because it mainly contains Chlorophyll d (Chl d) in the core complexes of PS I and PS II instead of the usually dominant Chl a. Furthermore, its light harvesting system has a structure also different from other cyanobacteria. It has both, a membrane-internal chlorophyll containing antenna and a membrane-external phycobiliprotein (PBP) complex. The first one binds Chl d and is structurally analogous to CP43. The latter one has a rod-like structure consisting of three phycocyanin (PC) homohexamers and one heterohexamer containing PC and allophycocyanin (APC). In this paper, we give an overview on the investigations of excitation energy transfer (EET) in this PBP-light-harvesting system and of charge separation in the photosystem II (PS II) reaction center of A. marina performed at the Technische Universität Berlin. Due to the unique structure of the PBP antenna in A. marina, this EET occurs on a much shorter overall time scale than in other cyanobacteria. We also briefly discuss the question of the pigment composition in the reaction center (RC) of PS II and the nature of the primary donor of the PS II RC.

摘要

海洋聚球藻是一种独特的蓝细菌,因为它的 PS I 和 PS II 核心复合物中主要含有叶绿素 d(Chl d),而不是通常占主导地位的叶绿素 a。此外,它的光捕获系统的结构也与其他蓝细菌不同。它既有膜内含叶绿素的天线,也有膜外的藻胆蛋白(PBP)复合物。前者结合 Chl d,结构上类似于 CP43。后者具有棒状结构,由三个藻蓝蛋白(PC)同六聚体和一个包含 PC 和别藻蓝蛋白(APC)的异六聚体组成。本文概述了在柏林工业大学对海洋聚球藻的 PBP 光捕获系统中的激发能量转移(EET)和光合作用系统 II(PS II)反应中心中的电荷分离进行的研究。由于海洋聚球藻中 PBP 天线的独特结构,这种 EET 的发生时间尺度比其他蓝细菌要短得多。我们还简要讨论了 PS II 反应中心中色素组成和 PS II RC 中初级供体的性质的问题。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验