Link T A, Schägger H, von Jagow G
FEBS Lett. 1986 Aug 11;204(1):9-15. doi: 10.1016/0014-5793(86)81378-3.
The interaction of the protein subunits of the bc1 complex from beef heart is analysed on the basis of protein chemical data and of secondary structure predictions suggesting a large number of amphipathic helices. Electrostatic interactions, i.e. helix-dipole interactions and ionic bonds, may play a major role in the stabilisation of the arrangement of the subunits within the multi-protein complex, formation of subcomplexes and maintenance of the steric strain of cytochrome b. A model of the heme-carrying 'core' of cytochrome b, i.e. of helices II-V, is presented consisting of a twisted '4-alpha-helical' bundle held together by helix-dipole interactions and stabilised by the interaction with other protein subunits of the bc1 complex.
基于蛋白质化学数据和二级结构预测（提示存在大量两亲性螺旋），对牛心bc1复合物的蛋白质亚基间相互作用进行了分析。静电相互作用，即螺旋偶极相互作用和离子键，可能在多蛋白复合物中亚基排列的稳定、亚复合物的形成以及细胞色素b空间应变的维持中起主要作用。本文提出了细胞色素b的携带血红素“核心”（即螺旋II-V）的模型，该模型由一个扭曲的“4-α-螺旋”束组成，通过螺旋偶极相互作用维系在一起，并通过与bc1复合物其他蛋白质亚基的相互作用得以稳定。
