Crystallographic Studies on Cytochrome c Peroxidase

这个项目的总体长期目标是了解细胞色素c过氧化物酶(CCP)的结构和功能。它是研究较彻底的血红素酶之一，天然蛋白质的X射线结构及其活性中间体化合物I已知的分辨率很高。CCP为研究血红蛋白之间的电子传递和氧-氧键的激活提供了一个理想的系统。许多有助于电子传递和能量传递过程的成分是含有血红素的酶，通常是多组分的复杂的膜结合组件，研究起来非常困难。CCP的优点是其相对较小的尺寸和易于结晶。尽管定点突变和单晶X射线衍射相结合的技术使许多研究路线成为可能，但德劳特博士过去的工作和现在提出的工作可以被描述为两条独立但最终收敛的实验路线。

The overall long term goal of this project is to understand the structure and function of cytochrome c peroxidase (CCP). It is one of the more thoroughly studied heme enzymes and the X-ray structure of the native protein, as well as its reactive intermediate, compound I, are known at high resolution. CCP offers an ideal system for the study of electron transport between hemeproteins and the activation of oxygen-oxygen bonds. Many of the components contributing to electron transport and energy transduction processes are heme-containing enzymes, usually multi-component, complex membrane-bound assemblies which are exceedingly difficult to study. The advantage of CCP is its relatively small size and ready crystallizability. Although many lines of investigation are made possible by the availbility of the combined techniques of site-directed mutagenesis and single crystal X-ray diffraction, Dr. Kraut's past work and that proposed now may be described as two separate but ultimately convergent experimental paths.***//