Kutuzov M A, Shmukler B E, Zargarov A A, Telezhinskaia I N, Levina N B, Zolotarev A S, Abdulaev N G
Bioorg Khim. 1990 Sep;16(9):1218-35.
Analysis of the Chloroflexus aurantiacus reaction centre (RC) using both protein and recombinant DNA techniques resulted in determination of its polypeptide composition and the primary structures of its two subunits. A model of the polypeptide chains' folding in the membrane is suggested based on: i) homology between L- and M-subunits of Chloroflexus aurantiacus RC and their counterparts in purple bacteria; ii) comparison of their hydropathy plots, and iii) data on the tertiary structures of purple bacteria RCs. The role of a number of functionally important amino acid residues in the RC electron transport activity is discussed. Limited proteolysis of the RC under non-denaturing conditions was used to determine the contribution of the N-terminal regions to its thermal stability.
利用蛋白质和重组DNA技术对橙色绿屈挠菌反应中心（RC）进行分析，确定了其多肽组成及其两个亚基的一级结构。基于以下几点提出了膜中多肽链折叠的模型：i）橙色绿屈挠菌RC的L亚基和M亚基与其在紫色细菌中的对应亚基之间的同源性；ii）它们的亲水性图谱比较；iii）紫色细菌RCs三级结构的数据。讨论了许多功能重要的氨基酸残基在RC电子传递活性中的作用。在非变性条件下对RC进行有限的蛋白酶解，以确定N端区域对其热稳定性的贡献。
