Ruban A V, Horton P, Robert B
Robert Hill Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
Biochemistry. 1995 Feb 21;34(7):2333-7. doi: 10.1021/bi00007a029.
Resonance Raman spectroscopy was performed on photosystem II light-harvesting complex (LHCII) in trimeric and oligomeric states with various excitation conditions. From these studies, it can be concluded that the structure of LHCII is altered during the trimer/oligomer transition. These structural changes affect the conformation of a population of carotenoid within the complex, which becomes twisted in the oligomeric form. Moreover, the interactions assumed by a chlorophyll a and a chlorophyll b are modified during the oligomerization process. This induces the formation of an H-bond to a formyl group of a chlorophyll b molecule and to a keto group of a chlorophyll a molecule. The extent to which these H-bonds to chlorophyll relate to the formation of the quencher cannot yet be precisely established. However, the structural changes they evidence may play a role in the control of the energy flux by LHCII complexes.
利用共振拉曼光谱技术,在不同激发条件下对三聚体和寡聚体状态的光系统II捕光复合物(LHCII)进行了研究。从这些研究中可以得出结论,LHCII的结构在三聚体/寡聚体转变过程中发生了改变。这些结构变化影响了复合物中类胡萝卜素群体的构象,其在寡聚体形式中发生扭曲。此外,叶绿素a和叶绿素b之间的相互作用在寡聚化过程中发生了改变。这诱导了与叶绿素b分子的甲酰基和叶绿素a分子的酮基形成氢键。这些与叶绿素的氢键与猝灭剂形成的关联程度尚未能精确确定。然而,它们所证明的结构变化可能在LHCII复合物对能量通量的控制中发挥作用。