Spectroscopic, electrochemical, and kinetic trends in Fe(III)–thiolate disproportionation near physiologic pH

In addition to its primary oxygen-atom-transfer function, cysteamine dioxygenase (ADO) exhibits a relatively understudied anaerobic disproportionation reaction (ADO-Fe(III)-SR → ADO-Fe(II) + ½ RSSR) with its native substrates. Inspired by ADO disproportionation reactivity, we employ [Fe(tacn)Cl₃] (tacn = 1,4,7-triazacyclononane) as a precursor for generating Fe(III)–thiolate model complexes in buffered aqueous media. A series of Fe(III)–thiolate model complexes are generated in situ using aqueous [Fe(tacn)Cl₃] and thiol-containing ligands cysteamine, penicillamine, mercaptopropionate, cysteine, cysteine methyl ester, N-acetylcysteine, and N-acetylcysteine methyl ester. We observe trends in UV–Vis and electron paramagnetic resonance (EPR) spectra, disproportionation rate constants, and cathodic peak potentials as a function of thiol ligand. These trends will be useful in rationalizing substrate-dependent Fe(III)–thiolate disproportionation reactions in metalloenzymes.