Berry Edward A, De Bari Heather, Huang Li-Shar
Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Biochim Biophys Acta. 2013 Nov-Dec;1827(11-12):1258-77. doi: 10.1016/j.bbabio.2013.04.006. Epub 2013 Apr 25.
X-ray crystal structures of bc1 complexes obtained over the last 15 years have provided a firm structural basis for our understanding of the complex. For the most part there is good agreement between structures from different species, different crystal forms, and with different inhibitors bound. In this review we focus on some of the remaining unexplained differences, either between the structures themselves or the interpretations of the structural observations. These include the structural basis for the motion of the Rieske iron-sulfur protein in response to inhibitors, a possible conformational change involving tyrosine132 of cytochrome (cyt) b, the presence of cis-peptides at the beginnings of transmembrane helices C, E, and H, the structural insight into the function of the so-called "Core proteins", different modelings of the retained signal peptide, orientation of the low-potential heme b, and chirality of the Met ligand to heme c1. This article is part of a Special Issue entitled: Respiratory complex III and related bc complexes.
过去15年里获得的bc1复合物的X射线晶体结构为我们理解该复合物提供了坚实的结构基础。在很大程度上，来自不同物种、不同晶体形式以及结合不同抑制剂的结构之间存在良好的一致性。在这篇综述中，我们关注一些仍然无法解释的差异，这些差异要么存在于结构本身之间，要么存在于对结构观察结果的解释中。这些差异包括 Rieske 铁硫蛋白响应抑制剂时运动的结构基础、细胞色素（cyt）b的酪氨酸132可能发生的构象变化、跨膜螺旋C、E和H起始处顺式肽的存在、对所谓“核心蛋白”功能的结构洞察、保留信号肽的不同建模、低电位血红素b的方向以及血红素c1的甲硫氨酸配体的手性。本文是名为：呼吸复合物III及相关bc复合物的特刊的一部分。
