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The synthesis of four new Fe II (N 4 S(thiolate)) complexes as models of the thiol dioxygenases are described. They are composed of derivatives of the neutral, tridentate ligand triazacyclononane (R 3 TACN; R = Me, iPr) and 2-aminobenzenethiolate (abt x ; X = H, CF 3 ), a non-native substrate for thiol dioxygenases. The coordination number of these complexes depends on the identity of the TACN derivative, giving 6-coordinate (6-coord) complexes for Fe II (Me 3 TACN)(abt x )(OTf) (1: X = H; 2: X = CF 3 ) and 5-coordinate (5-coord) complexes for [Fe II (iPr 3 TACN)(abt x )](OTf) (3: X = H; 4: X = CF 3 ). Complexes 1-4 were examined by UV-vis, 1 H/ 19 F NMR, and Mössbauer spectroscopies, and density functional theory (DFT) calculations were employed to support the data. Mössbauer spectroscopy reveals that the 6-coord 1-2 and 5-coord 3- 4 exhibit distinct spectra, and these data are compared with that for cysteine-bound CDO, helping to clarify the coordination environment of the cys-bound Fe II active site. Reaction of 1 or 2 with O 2 at -95 °C leads to S-oxygenation of the abt ligand, and in the case of 2, a rare di(sulfinato)-bridged complex, [Fe 2  III (μ-O)((2-NH 2 ) p-CF 3 C 6 H 3 SO 2 ) 2 ](OTf) 2 ( 5), was obtained. Parallel enzymatic studies on the CDO variant C93G were carried out with the abt substrate and show that reaction with O 2 leads to disulfide formation, as opposed to S-oxygenation. The combined model and enzyme studies show that the thiol dioxygenases can operate via a 6-coord Fe II center, in contrast to the accepted mechanism for nonheme iron dioxygenases, and that proper substrate chelation to Fe appears to be critical for S-oxygenation.

journal of the american chemical society

Structures, Spectroscopic Properties, and Dioxygen Reactivity of 5- and 6-Coordinate Nonheme Iron(II) Complexes: A Combined Enzyme/Model Study of Thiol Dioxygenases