The structure, function and dynamics of photosystem two
The structure, function and dynamics of photosystem two
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DOI：
10.1034/j.1399-3054.1997.1000408.x
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发表时间：
1997-08-01
影响因子：
6.4
通讯作者：
Hankamer, B
中科院分区：
文献类型：
--
作者：
Barber, J;Nield, J;Hankamer, B
现代光合作用研究的最大挑战之一是充分阐明光系统2（PSII）的结构和功能特性。这种水-质体醌氧化还原酶位于由超过25个亚基组成的膜复合物中。综述了构成PSII核心的所有已知亚基的一级和二级结构。这些亚基如何相互作用，在体内产生PSII的三级和四级结构尚未完全了解。然而，电子显微镜通过单粒子分析和电子晶体学帮助填补了我们知识中的这一空白。这些研究表明，活跃的PSII是二聚体，虽然这种寡聚状态的功能意义还不清楚。此外，阐明的光系统一（PSI）的结构，通过X-射线晶体学揭示的功能，这可能是相关的PSII结构。具有CP 43的D1蛋白和具有CP 47的D2蛋白（在每种情况下总计11个跨膜螺旋）似乎极有可能与PsaA和PsaB的组织具有结构相似性。很可能D1蛋白的周转是通过相对容易地从PSII核心的这种排列中去除CP 43来帮助的。
One of the greatest challenges in modern photosynthesis research is to elucidate fully the structural and functional properties of photosystem two (PSII). This water-plastoquinone oxidoreductase is located in a membrane complex composed of more than 25 subunits. The primary and secondary structures of all known subunits which constitute the central core of PSII are reviewed. How these subunits interact with each other to produce the tertiary and quaternary structure of PSII in vivo is not fully understood. However, electron microscopy is helping to fill this gap in our knowledge both by single particle analysis and electron crystallography. These studies suggest that active PSII is dimeric, although the functional significance of this oligomeric state is not yet understood. Moreover, the elucidation of the structure of photosystem one (PSI) by X-ray crystallography has revealed features which are likely to be relevant to PSII structure. It seems highly likely that the D1 protein with CP43 and D2 protein with CP47 (summing 11 transmembrane helices in each case) will have structural similarities to the organisation of PsaA and PsaB. It is likely that the turnover of the D1 protein is aided by the relatively easy removal of CP43 from this arrangement of the PSII core.