Spectroscopic and Theoretical Investigation of High-Spin Square-Planar and Trigonal Fe(II) Complexes Supported by Fluorinated Alkoxides.

The electronic structures and spectroscopic behavior of three high-spin FeII complexes of fluorinated alkoxides were studied: square-planar {K(DME)2}2[Fe(pinF)2] (S) and quasi square-planar {K(C222)}2[Fe(pinF)2] (S') and trigonal-planar {K(18C6)}[Fe(OC4F9)3] (T) where pinF = perfluoropinacolate and OC4F9 = tris-perfluoro-t-butoxide. The zero-field splitting (ZFS) and hyperfine structure parameters of the S = 2 ground states were determined using field-dependent 57Fe Mössbauer and high-field and -frequency electron paramagnetic resonance (HFEPR) spectroscopies. The spin Hamiltonian parameters were analyzed with crystal field theory and corroborated by density functional theory (DFT) and ab initio complete active space self-consistent field (CASSCF) calculations. Whereas the ZFS tensor of S has a small rhombicity, E/D = 0.082, and a positive D = 15.17 cm-1, T exhibits a negative D = -9.16 cm-1 and a large rhombicity, E/D = 0.246. Computational investigation of the structural factors suggests that the ground-state electronic configuration and geometry of T's Fe site are determined by the interaction of [Fe(OC4F9)3]- with {K(18C6)}+. In contrast, two distinct countercations of S/S' have a negligible influence on their [Fe(pinF)2]2- moieties. Instead, the distortions in S' are likely induced by the chelate ring conformation change from δλ, observed for S, to the δδ conformation, determined for S'.

Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor.

Acetone carboxylases (ACs) catalyze the metal- and ATP-dependent conversion of acetone and bicarbonate to form acetoacetate. Interestingly, two homologous ACs that have been biochemically characterized have been reported to have different metal complements, implicating different metal dependencies in catalysis. ACs from proteobacteria Xanthobacter autotrophicus and Aromatoleum aromaticum share 68% sequence identity but have been proposed to have different catalytic metals. In this work, the two ACs were expressed under the same conditions in Escherichia coli and were subjected to parallel chelation and reconstitution experiments with Mn(II) or Fe(II). Electron paramagnetic and Mössbauer spectroscopies identified signatures, respectively, of Mn(II) or Fe(II) bound at the active site. These experiments showed that the respective ACs, without the assistance of chaperones, second metal sites, or post-translational modifications facilitate correct metal incorporation, and despite the expected thermodynamic preference for Fe(II), each preferred a distinct metal. Catalysis was likewise associated uniquely with the cognate metal, though either could potentially serve the proposed Lewis acidic role. Subtle differences in the protein structure are implicated in serving as a selectivity filter for Mn(II) or Fe(II).IMPORTANCEThe Irving-Williams series refers to the predicted stabilities of transition metal complexes where the observed general stability for divalent first-row transition metal complexes increase across the row. Acetone carboxylases (ACs) use a coordinated divalent metal at their active site in the catalytic conversion of bicarbonate and acetone to form acetoacetate. Highly homologous ACs discriminate among different divalent metals at their active sites such that variations of the enzyme prefer Mn(II) over Fe(II), defying Irving-Williams-predicted behavior. Defining the determinants that promote metal discrimination within the first-row transition metals is of broad fundamental importance in understanding metal-mediated catalysis and metal catalyst design.