Department of Biochemistry, University of Oxford, Oxford, UK.
FEBS J. 2011 Nov;278(22):4170-8. doi: 10.1111/j.1742-4658.2011.08376.x. Epub 2011 Oct 20.
Cytochromes c are widespread respiratory proteins characterized by the covalent attachment of heme. The formation of c-type cytochromes requires, in all but a few exceptional cases, the formation of two thioether bonds between the two cysteine sulfurs in a -CXXCH- motif in the protein and the vinyl groups of heme. The vinyl groups of the heme are not particularly activated and therefore the addition reaction does not physiologically occur spontaneously in cells. There are several diverse post-translational modification systems for forming these bonds. Here, we describe the complex multiprotein cytochrome c maturation (Ccm) system (in Escherichia coli comprising the proteins CcmABCDEFGH), also called System I, that performs the heme attachment. System I is found in plant mitochondria, archaea and many Gram-negative bacteria; the systems found in other organisms and organelles are described elsewhere in this minireview series.
细胞色素 c 是广泛存在的呼吸蛋白,其特征是通过共价键连接血红素。除了少数特殊情况外,所有 c 型细胞色素的形成都需要在蛋白质中的 -CXXCH- 模体中两个半胱氨酸硫原子与血红素的乙烯基之间形成两个硫醚键。血红素的乙烯基没有特别活化,因此在细胞中,该加成反应不会自发发生。有几种不同的翻译后修饰系统用于形成这些键。在这里,我们描述了复杂的多蛋白细胞色素 c 成熟(Ccm)系统(在大肠杆菌中包括蛋白 CcmABCDEFGH),也称为系统 I,该系统执行血红素附着。系统 I 存在于植物线粒体、古菌和许多革兰氏阴性细菌中;在其他生物体和细胞器中发现的系统在本综述系列的其他地方进行了描述。