A Dinuclear Iron(II) Persulfide Complex Reacts with O2 to Give Sulfite: Relevance to Persulfide Dioxygenases.

Persulfides (RSSH) have been proposed as key players in biochemical transformations that often involve iron, including iron-sulfur cluster assembly, H2S regulation, post translational modifications, and mitochondrial sulfur oxidation. An example of the latter is found in the O2-mediated oxidation of glutathione persulfide to sulfite dianion (SO32-) catalyzed by ETHE1, a nonheme iron persulfide dioxygenase (PDO). The iron-mediated mechanism of persulfide oxidation by PDOs remains poorly understood, and there are no synthetic analogues to date. Herein, we report the synthesis, characterization, and O2 reactivity of a rare iron(II)-alkylpersulfide complex. The adamantyl persulfide anion (AdSS-) was isolated and characterized by X-ray diffraction as a complex with potassium 18-crown-6 [K(18-crown-6)][AdSS], and employed in the synthesis of a new dinuclear iron(II) complex, [(FeII(Me3TACN))2(μ2-SSAd)3][OTf] (1). Complex 1 was characterized by single crystal X-ray diffraction (XRD), UV-vis, 1H/19F NMR, and 57Fe Mössbauer spectroscopy. Reaction of 1 with O2 in CH3CN affords a diiron(III) oxo-bridged complex [(FeIII(Me3TACN))2(μ-O)(μ2-SO4)(μ2-SO3Ad)][OTf] (2) identified by XRD, and SO32- (∼0.5 equiv per Fe2). Isotopic labeling studies using 18O2 and H218O, supported by control experiments and ESI-MS analysis, indicate that SO32- production proceeds via an iron-centered S-oxygenation mechanism similar to that proposed for persulfide dioxygenases.