Structure analysis and characterization of the LH1-RC complex induced by metal ions

测定了细菌光合作用光收集反应中心核心配合物（LH1-RC）的晶体结构。结构显示LH1配合物围绕RC闭合排列，LH1 BChl a分子形成部分重叠的环，与LH2中的B850分子相比，Mg-Mg间距更短。本文首次为封闭LH1复合体中泛素通路的可能提供了结构证据。确定了Ca2+结合位点。醌转运、Ca2+调控和LH1与RC相互作用的分子机制描述如下。该研究结果发表在《自然》杂志上。

The crystal structure of a bacterial photosynthetic light-harvesting-reaction center core complex (LH1-RC) has been determined. The structure reveals a closed arrangement of LH1 complex around the RC, and the LH1 BChl a molecules form a partially overlapping ring with a shorter Mg-Mg spacing compared with that of B850 in LH2. Structural evidence is for first time provided for the possible ubiquinone pathway in the closed LH1 complex. The Ca2+-binding sites are identified. Molecular mechanisms of quinone transport, Ca2+-regulation and interaction between LH1 and RC are described below. The result has been published in Nature.