Structure of an Open Conformation of Cytochrome P450 Reductase MS #M8:07868 Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450
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Running title: Structure of an Open Conformation of Cytochrome P450 Reductase These authors contributed equally to the work. Address correspondence to: Lucy Waskell, Department of Anesthesiology, University of Michigan and Veterans Affairs Medical Research Center, 2215 Fuller Rd. Ann Arbor, Michigan 48105, Tel: 734-8455858, E-mail: [email protected] or Jung-Ja P. Kim, Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Rd., Milwaukee, Wisconsin 53226, Tel: 414-9558479, E-mail: [email protected]
منابع مشابه
Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.
Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase system that participates in the metabolism of endo- and xenobiotic compounds in mammals. Available...
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تاریخ انتشار 2009