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P. Ross Wilderman, Sean C. Gay, Hyun-Hee Jang, Qinghai Zhang, C. David Stout and James R. Halpert Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein–ligand interactions based on crystal structures of the ligand-bound enzyme The FEBS Journal 279

Version of Record online: 25 NOV 2011 | DOI: 10.1111/j.1742-4658.2011.08411.x

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A systematic investigation was undertaken by site-directed mutagenesis of unique residue-residue interactions predicted from crystal structures of a closed conformation of cytochrome P450 2B4 in complex with 4-(4-chlorophenyl)imidazole or an expanded conformation in complex with bifonazole. Several mutants far from the active site exhibited profound changes in susceptibility to inhibition by the two compounds and/or catalytic efficiency with several substrates.

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