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Michael G Joyce, Idorenyin S. Ekanem, Olivier Roitel, Adrian J. Dunford, Rajasekhar Neeli, Hazel M. Girvan, George J. Baker, Robin A. Curtis, Andrew W. Munro and David Leys The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3 The FEBS Journal 279

Version of Record online: 16 MAR 2012 | DOI: 10.1111/j.1742-4658.2012.08544.x

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P450 BM3 is a model enzyme in the P450 superfamily. The structure of its FAD/NADPH-binding domain represents the final piece of the structural jigsaw for this biotechnologically important enzyme. Wild-type FAD domain is predominantly dimeric, but a variant containing the C773A mutation prevented disulfide bond formation, produced monomeric protein and enabled crystallization/structural elucidation of ligand-free and NADP+-bound FAD domain forms.

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