Structural Basis of the Divergent Oxygenation Reactions Catalyzed by the Rieske Nonheme Iron Oxygenase Carbazole 1,9a-Dioxygenase

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    Comparison of the molecular surface of the substrate-binding pocket of wild-type carbazole 1,9a-dioxygenase and its I262V derivative in chain B (Fig. S1); comparison of the molecular surface of the substrate-binding pocket of wild-type carbazole 1,9a-dioxygenase and its F275W derivative in chain B (Fig. S2); electron density map of the substrate-binding pocket in chain C of the carbazole 1,9a-dioxygenase F275W derivative with bound fluorene and omit map of the F275W derivative with the FN flipped 180° around its long axis from its original position, in which FN was fit to the electron density map (Fig. S3); omparison of the molecular surface of the substrate-binding pocket of wild-type carbazole 1,9a-dioxygenase and its Q282N derivative in chain B (Fig. S4); comparison of the molecular surface of the substrate-binding pocket of wild-type carbazole 1,9a-dioxygenase and its Q282Y derivative in chain B (Fig. S5); hierarchical clustering analysis based on the pairwise root-mean-square-deviation (RMSD) distance matrix using each chain in the determined crystal structures with and without substrate (Fig. S6).

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