Crystallographic Studies on Cytochrome c Peroxidase

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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.***//