STRUCTURE OF THE CYTOCHROME C PEROXIDASE INTERMEDIATE COMPOUND I

Stanford University, Stanford CA

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Cytochrome c peroxidase (CCP) is an intercellular heme enzyme that oxidizes substrates in a multi-step reaction. The iron atom in Compound I is purportedly oxidized from +3 to +4 forming an oxyferryl center in the first step. Attempts to collect x-ray diffraction data from the intermediate compound I have been complicated due to auto-reduction of the complex from the incident x-rays We have been studying the auto-reduction rates using VIS spectroscopy. We have determined that at 67 K, ~4 exposures can be collected from moderately sized crystals to 1.3 A resolution. The temperature is just above the freezing point of nitrogen, while preserving 85% of Compound 1. Methods will be developed to use the robot to screen and collect data from a series of crystals to build a complete data set.