Abstract
This chapter focuses on the crystallization studies of NADPH-cytochrome P450 reductase (CPR). NADPH-cytochrome P450 reductase is an essential component of the microsomal cytochrome P450 monooxygenase system. It is an integral membrane protein that catalyzes the transfer of electrons from NADPH to cytochrome P450 in the oxidative metabolism of the endogenous and exogenous substrates. The three-dimensional structure of CPR by X-ray analysis can reveal, at the molecular level, the interactions among the pyridine nucleotide NADPH, the flavins, and the polypeptide chain of CPR, and the spatial relationship among the different domains of CPR that allow for efficient electron transfer. In addition, the nature of the binding site for cytochrome P450 can be identified, providing the structural basis for the ability of CPR to interact with scores of different cytochromes P450. Obtaining crystals of CPR establishes the basis for the full structural analysis of CPR by X-ray diffraction methods. The crystallization conditions obtained from the CPR studies can be used as a starting point for crystallization of other FMN- and FAD-containing proteins, such as nitric oxide synthase.
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