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

测定了细菌光合作用捕光反应中心核心复合体(LH1-RC)的晶体结构。该结构揭示了LH1络合物在RC周围的封闭排列，与LH2中的B850相比，LH1的BCHLα分子形成了一个部分重叠的环，其镁-镁间距较小。首次为闭合LH1复合体中可能的泛醌途径提供了结构证据。确定了钙结合部位。下面描述了苯醌转运、钙调节以及LH1和RC之间相互作用的分子机制。这项研究结果已发表在《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.