The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength

The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength

NADPH-cytochrome P450 reductase (CPR) is a redox partner of microsomal cytochromes P450 and is a prototype of the diflavin reductase family. CPR contains 3 distinct functional domains: a FMN-binding domain (acceptor reduction), a linker (hinge), and a connecting/FAD domain (NADPH oxidation). It has...

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Bibliographic Details
Main Authors: Diana Campelo, Thomas Lautier, Philippe Urban, Francisco Esteves, Sophie Bozonnet, Gilles Truan, Michel Kranendonk
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-10-01
Series:Frontiers in Pharmacology
Subjects:
diflavin reductase
protein dynamics
multidomain proteins
conformational exchange
electron transfer
protein–protein interaction
Online Access:http://journal.frontiersin.org/article/10.3389/fphar.2017.00755/full

Internet

http://journal.frontiersin.org/article/10.3389/fphar.2017.00755/full

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