Ruthenium(II) PNN complexes depolymerize many polyesters into diols and polycarbonates into glycols plus methanol via hydrogenation. Notably, polyesters with two methylene units between ester linkages depolymerize to carboxylic acids rather than diols. This methodology represents a new approach for producing useful chemicals from waste plastics.

A new family of highly active ethylene tri-/tetramerization catalysts based on N-phosphinoamidinechromium complexes has been investigated. The 1-hexene to 1-octene molar ratio can be tuned from 140 to 1.5 by varying the steric environment around the chromium center, and product purities are very good to excellent. Precatalyst tridentate coordination effectively shuts down catalytic activity, suggesting that THF abstraction from the chromium center by the Lewis acidic aluminum activator is necessary to achieve an active catalyst system.

The active sites of metalloenzymes that catalyze O-dependent reactions generally contain iron or copper ions. However, several enzymes are capable of activating O at manganese or nickel centers instead, and a handful of dioxygenases exhibit activity when substituted with cobalt. This minireview summarizes the catalytic properties of oxygenases and oxidases with mononuclear Mn, Co, or Ni active sites, including oxalate-degrading oxidases, catechol dioxygenases, and quercetin dioxygenase. In addition, recent developments in the O reactivity of synthetic Mn, Co, or Ni complexes are described, with an emphasis on the nature of reactive intermediates featuring superoxo-, peroxo-, or oxo-ligands. Collectively, the biochemical and synthetic studies discussed herein reveal the possibilities and limitations of O activation at these three "overlooked" metals.

A nonheme Fe(II) complex (1) that models substrate-bound cysteine dioxygenase (CDO) reacts with O2 at −80 °C to yield a purple intermediate (2). Analysis with spectroscopic and computational methods determined that 2 features a thiolate-ligated Fe(III) center bound to a superoxide radical, mimicking the putative structure of a key CDO intermediate.

The substitution of non-native metal ions into metalloenzyme active sites is a common strategy for gaining insights into enzymatic structure and function. For some nonheme iron dioxygenases, replacement of the Fe(ii) center with a redox-active, divalent transition metal (e.g., Mn, Co, Ni, Cu) gives rise to an enzyme with equal or greater activity than the wild-type enzyme. In this manuscript, we apply this metal-substitution approach to synthetic models of the enzyme cysteine dioxygenase (CDO). CDO is a nonheme iron dioxygenase that initiates the catabolism of l-cysteine by converting this amino acid to the corresponding sulfinic acid. Two mononuclear Co(ii) complexes (3 and 4) have been prepared with the general formula [Co(Tp)(CysOEt)] (R = Ph (3) or Me (4); Tp = hydrotris(pyrazol-1-yl)borate substituted with R-groups at the 3- and 5-positions, and CysOEt is the anion of l-cysteine ethyl ester). These Co(ii) complexes mimic the active-site structure of substrate-bound CDO and are analogous to functional iron-based CDO models previously reported in the literature. Characterization with X-ray crystallography and/or H NMR spectroscopy revealed that 3 and 4 possess five-coordinate structures featuring facially-coordinating Tp and S,N-bidentate CysOEt ligands. The electronic properties of these high-spin (S = 3/2) complexes were interrogated with UV-visible absorption and X-band electron paramagnetic resonance (EPR) spectroscopies. The air-stable nature of complex 3 replicates the inactivity of cobalt-substituted CDO. In contrast, complex 4 reversibly binds O at reduced temperatures to yield an orange chromophore (4-O). Spectroscopic (EPR, resonance Raman) and computational (density functional theory, DFT) analyses indicate that 4-O is a S = 1/2 species featuring a low-spin Co(iii) center bound to an end-on (η) superoxo ligand. DFT calculations were used to evaluate the energetics of key steps in the reaction mechanism. Collectively, these results have elucidated the role of electronic factors (e.g., spin-state, d-electron count, metal-ligand covalency) in facilitating O activation and S-dioxygenation in CDO and related models.