Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
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DOI：
10.1038/35082000
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发表时间：
2001-06-21
期刊：
影响因子：
64.8
通讯作者：
Krauss, N
中科院分区：
文献类型：
--
作者：
Jordan, P;Fromme, P;Krauss, N
地球上的生命依靠光合作用，即将太阳的光能转化为化学能。在植物中，绿藻和蓝藻，这一过程是由位于类囊体光合膜上的两个大的蛋白质辅助因子复合物，光系统I和II的合作驱动的。本文描述的嗜热蓝藻长聚球菌光系统I的晶体结构提供了12个蛋白质亚基和127个辅助因子的原子细节图，包括96个叶绿素，2个叶绿醌，3个Fe4S4簇，22个类胡萝卜素，4个脂质，1个推测的Ca2+离子和201个水分子。蛋白质和辅助因子及其相互作用的结构信息为理解光系统I在光捕获和电子转移方面的高效率是如何实现的提供了基础。
Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved.