Suppr超能文献

植物光系统II反应中心8埃分辨率的三维结构。

Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution.

作者信息

Rhee K H, Morris E P, Barber J, Kühlbrandt W

机构信息

Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie, Frankfurt am Main, Germany.

出版信息

Nature. 1998 Nov 19;396(6708):283-6. doi: 10.1038/24421.

Abstract

Photosystem II is a multisubunit enzyme complex involved in plant photosynthesis. It uses solar energy to catalyse the breakdown of water to reducing equivalents and molecular oxygen. Native photosystem II comprises more than 25 different subunits, and has a relative molecular mass of more than 600K. Here we report the three-dimensional structure of a photosystem II subcomplex, containing the proteins D1, D2, CP47 and cytochrome b-559, determined by electron crystallography. This CP47 reaction centre, which has a relative molecular mass of 160K, can perform light-mediated energy and electron-transfer reactions but is unable to oxidize water. The complex contains 23 transmembrane alpha-helices, of which 16 have been assigned to the D1, D2 and CP47 proteins. The arrangement of these helices is remarkably similar to that of the helices in the reaction centres of purple bacteria and of plant photosystem I, indicating a common evolutionary origin for these assemblies. The map suggests that redox cofactors in the D1-D2 complex are located in positions analogous to those in the bacterial reaction centre, but the distance between the chlorophylls corresponding to the bacterial 'special pair' is significantly larger.

摘要

光系统II是一种参与植物光合作用的多亚基酶复合物。它利用太阳能催化水分解为还原当量和分子氧。天然光系统II由25种以上不同的亚基组成,相对分子质量超过600K。在此,我们报告了通过电子晶体学确定的光系统II亚复合物的三维结构,该亚复合物包含蛋白质D1、D2、CP47和细胞色素b-559。这个相对分子质量为160K的CP47反应中心能够进行光介导的能量和电子转移反应,但无法氧化水。该复合物包含23个跨膜α螺旋,其中16个已被确定属于D1、D2和CP47蛋白。这些螺旋的排列与紫色细菌反应中心和植物光系统I中的螺旋排列非常相似,表明这些组件有共同的进化起源。图谱显示,D1-D2复合物中的氧化还原辅因子位于与细菌反应中心类似的位置,但与细菌“特殊对”相对应的叶绿素之间的距离明显更大。

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