Lithium superoxide encapsulated in a benzoquinone anion matrix.

Lithium peroxide is the crucial storage material in lithium-air batteries. Understanding the redox properties of this salt is paramount toward improving the performance of this class of batteries. Lithium peroxide, upon exposure to p-benzoquinone (p-C6H4O2) vapor, develops a deep blue color. This blue powder can be formally described as [Li2O2][Formula: see text] [LiO2][Formula: see text] {Li[p-C6H4O2]}0.7, though spectroscopic characterization indicates a more nuanced structural speciation. Infrared, Raman, electron paramagnetic resonance, diffuse-reflectance ultraviolet-visible and X-ray absorption spectroscopy reveal that the lithium salt of the benzoquinone radical anion forms on the surface of the lithium peroxide, indicating the occurrence of electron and lithium ion transfer in the solid state. As a result, obligate lithium superoxide is formed and encapsulated in a shell of Li[p-C6H4O2] with a core of Li2O2 Lithium superoxide has been proposed as a critical intermediate in the charge/discharge cycle of Li-air batteries, but has yet to be isolated, owing to instability. The results reported herein provide a snapshot of lithium peroxide/superoxide chemistry in the solid state with redox mediation.

Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification.

Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide. They bear specialized "heme P460" cofactors that are cross-linked to their host polypeptides by a post-translationally modified lysine residue. Wild-type N. europaea cytochrome P460 may be isolated as a cross-link-deficient proenzyme following anaerobic overexpression in E. coli. When treated with peroxide, this proenzyme undergoes maturation to active enzyme with spectroscopic and catalytic properties that match wild-type cyt P460. This maturation reactivity requires no chaperones─it is intrinsic to the protein. This behavior extends to the broader cytochrome c'ß superfamily. Accumulated data reveal key contributions from the secondary coordination sphere that enable selective, complete maturation. Spectroscopic data support the intermediacy of a ferryl species along the maturation pathway.

Accelerating σ-Bond Metathesis at Sn(II) Centers.

Molecular main-group hydride catalysts are attractive as cheap and Earth-abundant alternatives to transition-metal analogues. In the case of the latter, specific steric and electronic tuning of the metal center through ligand choice has enabled the iterative and rational development of superior catalysts. Analogously, a deeper understanding of electronic structure-activity relationships for molecular main-group hydrides should facilitate the development of superior main-group hydride catalysts. Herein, we report a modular Sn-Ni bimetallic system in which we systematically vary the ancillary ligand on Ni, which, in turn, tunes the Sn center. This tuning is probed using Sn L1 XAS as a measure of electron density at the Sn center. We demonstrate that increased electron density at Sn centers accelerates the rate of σ-bond metathesis, and we employ this understanding to develop a highly active Sn-based catalyst for the hydroboration of CO2 using pinacolborane. Additionally, we demonstrate that engineering London dispersion interactions within the secondary coordination sphere of Sn allows for further rate acceleration. These results show that the electronics of main-group catalysts can be controlled without the competing effects of geometry perturbations and that this manifests in substantial reactivity differences.

Ionothermal Synthesis of Metal-Organic Frameworks Using Low-Melting Metal Salt Precursors.

Metal-organic frameworks (MOFs) are porous, crystalline materials constructed from organic linkers and inorganic nodes with myriad potential applications in chemical separations, catalysis, and drug delivery. A major barrier to the application of MOFs is their poor scalability, as most frameworks are prepared under highly dilute solvothermal conditions using toxic organic solvents. Herein, we demonstrate that combining a range of linkers with low-melting metal halide (hydrate) salts leads directly to high-quality MOFs without added solvent. Frameworks prepared under these ionothermal conditions possess porosities comparable to those prepared under traditional solvothermal conditions. In addition, we report the ionothermal syntheses of two frameworks that cannot be prepared directly under solvothermal conditions. Overall, the user-friendly method reported herein should be broadly applicable to the discovery and synthesis of stable metal-organic materials.

Electronic Structure of Ru26+ Complexes with Electron-Rich Anilinopyridinate Ligands.

Diruthenium paddlewheel complexes supported by electron-rich anilinopyridinate (Xap) ligands were synthesized in the course of the first in-depth structural and spectroscopic interrogation of monocationic [Ru2(Xap)4Cl]+ species in the Ru26+ oxidation state. Despite paramagnetism of the compounds, 1H NMR spectroscopy proved highly informative for determining the isomerism of the Ru25+ and Ru26+ compounds. While most compounds are found to have the polar (4,0) geometry, with all four Xap ligands in the same orientation, some synthetic procedures resulted in a mixture of (4,0) and (3,1) isomers, most notably in the case of the parent compound Ru2(ap)4Cl. The isomerism of this compound has been overlooked in previous reports. Electrochemical studies demonstrate that oxidation potentials can be tuned by the installation of electron donating groups to the ligands, increasing accessibility of the Ru26+ oxidation state. The resulting Ru26+ monocations were found to have the expected (π*)2 ground state, and an in-depth study of the electronic transitions by Vis/NIR absorption and MCD spectroscopies with the aid of TD-DFT allowed for the assignment of the electronic spectra. The empty δ* orbital is the major acceptor orbital for the most prominent electronic transitions. Both Ru25+ and Ru26+ compounds were studied by Ru K-edge X-ray absorption spectroscopy; however, the rising edge energy is insensitive to redox changes in the compounds due to the broad line shape observed for 4d transition metal K-edges. DFT calculations indicate the presence of ligand orbitals at the frontier level, suggesting that further oxidation beyond Ru26+ will be ligand-centered rather than metal-centered.

Iron Complexes of a Proton-Responsive SCS Pincer Ligand with a Sensitive Electronic Structure.

Sulfur/carbon/sulfur pincer ligands have an interesting combination of strong-field and weak-field donors, a coordination environment that is also present in the nitrogenase active site. Here, we explore the electronic structures of iron(II) and iron(III) complexes with such a pincer ligand, bearing a monodentate phosphine, thiolate S donor, amide N donor, ammonia, or CO. The ligand scaffold features a proton-responsive thioamide site, and the protonation state of the ligand greatly influences the reduction potential of iron in the phosphine complex. The N-H bond dissociation free energy, derived from the Bordwell equation, is 56 ± 2 kcal/mol. Electron paramagnetic resonance (EPR) spectroscopy and superconducting quantum interference device (SQUID) magnetometry measurements show that the iron(III) complexes with S and N as the fourth donors have an intermediate spin (S = 3/2) ground state with a large zero field splitting, and X-ray absorption spectra show a high Fe-S covalency. The Mössbauer spectrum changes drastically with the position of a nearby alkali metal cation in the iron(III) amido complex, and density functional theory calculations explain this phenomenon through a change between having the doubly occupied orbital as dz2 or dyz, as the former is more influenced by the nearby positive charge.

Direct Reduction of NO to N2O by a Mononuclear Nonheme Thiolate Ligated Iron(II) Complex via Formation of a Metastable {FeNO}7 Complex.

Addition of NO to a nonheme dithiolate-ligated iron(II) complex, FeII(Me3TACN)(S2SiMe2) (1), results in the generation of N2O. Low-temperature spectroscopic studies reveal a metastable six-coordinate {FeNO}7 intermediate (S = 3/2) that was trapped at -135 °C and was characterized by low-temperature UV-vis, resonance Raman, EPR, Mössbauer, XAS, and DFT studies. Thermal decay of the {FeNO}7 species leads to the evolution of N2O, providing a rare example of a mononuclear thiolate-ligated {FeNO}7 that mediates NO reduction to N2O without the requirement of any exogenous electron or proton sources.

Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.

The metallobiochemistry underlying the formation of the inorganic N-N-bond-containing molecules nitrous oxide (N2O), dinitrogen (N2), and hydrazine (N2H4) is essential to the lifestyles of diverse organisms. Similar reactions hold promise as means to use N-based fuels as alternative carbon-free energy sources. This review discusses research efforts to understand the mechanisms underlying biological N-N bond formation in primary metabolism and how the associated reactions are tied to energy transduction and organismal survival. These efforts comprise studies of both natural and engineered metalloenzymes as well as synthetic model complexes.

A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species.

Many bacteria contain cytoplasmic chemoreceptors that lack sensor domains. Here, we demonstrate that such cytoplasmic receptors found in 8 different bacterial and archaeal phyla genetically couple to metalloproteins related to ß-lactamases and nitric oxide reductases. We show that this oxygen-binding di-iron protein (ODP) acts as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable µ-peroxo adduct. Crystal structures of ODP from Td and the thermophile Thermotoga maritima (Tm) in the Fe[III]2-O22-, Zn[II], and apo states display differences in subunit association, conformation, and metal coordination that indicate potential mechanisms for sensing. In reconstituted systems, iron-peroxo ODP destabilizes the phosphorylated form of the receptor-coupled histidine kinase CheA, thereby providing a biochemical link between oxygen sensing and chemotaxis in diverse prokaryotes, including anaerobes of ancient origin.

An Isolable Mononuclear Palladium(I) Amido Complex.

Mononuclear Pd(I) species are putative intermediates in Pd-catalyzed reactions, but our knowledge about them is limited due to difficulties in accessing them. Herein, we report the isolation of a Pd(I) amido complex, [(BINAP)Pd(NHArTrip)] (BINAP = 2,2'-bis(diphenylphosphino)-1,1'-binaphthalene, ArTrip = 2,6-bis(2',4',6'-triisopropylphenyl)phenyl), from the reaction of (BINAP)PdCl2 with LiNHArTrip. This Pd(I) amido species has been characterized by X-ray crystallography, electron paramagnetic resonance, and multiedge Pd X-ray absorption spectroscopy. Theoretical study revealed that, while the three-electron-two-center π-interaction between Pd and N in the Pd(I) complex imposes severe Pauli repulsion in its Pd-N bond, pronounced attractive interligand dispersion force aids its stabilization. In accord with its electronic features, reactions of homolytic Pd-N bond cleavage and deprotonation of primary amines are observed on the Pd(I) amido complex.

Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.

All radical S-adenosylmethionine (radical-SAM) enzymes, including the noncanonical radical-SAM enzyme diphthamide biosynthetic enzyme Dph1-Dph2, require at least one [4Fe-4S](Cys)3 cluster for activity. It is well-known in the radical-SAM enzyme community that the [4Fe-4S](Cys)3 cluster is extremely air-sensitive and requires strict anaerobic conditions to reconstitute activity in vitro. Thus, how such enzymes function in vivo in the presence of oxygen in aerobic organisms is an interesting question. Working on yeast Dph1-Dph2, we found that consistent with the known oxygen sensitivity, the [4Fe-4S] cluster is easily degraded into a [3Fe-4S] cluster. Remarkably, the small iron-containing protein Dph3 donates one Fe atom to convert the [3Fe-4S] cluster in Dph1-Dph2 to a functional [4Fe-4S] cluster during the radical-SAM enzyme catalytic cycle. This mechanism to maintain radical-SAM enzyme activity in aerobic environments is likely general, and Dph3-like proteins may exist to keep other radical-SAM enzymes functional in aerobic environments.

Heme P460: A (Cross) Link to Nitric Oxide.

Ammonia-oxidizing bacteria (AOB) convert ammonia (NH3) to nitrite (NO2-) as their primary metabolism and thus provide a blueprint for the use of NH3 as a chemical fuel. The first energy-producing step involves the homotrimeric enzyme hydroxylamine oxidoreductase (HAO), which was originally reported to oxidize hydroxylamine (NH2OH) to NO2-. HAO uses the heme P460 cofactor as the site of catalysis. This heme is supported by seven other c hemes in each monomer that mediate electron transfer. Heme P460 cofactors are c-heme-based cofactors that have atypical protein cross-links between the peptide backbone and the porphyrin macrocycle. This cofactor has been observed in both the HAO and cytochrome (cyt) P460 protein families. However, there are differences; specifically, HAO uses a single tyrosine residue to form two covalent attachments to the macrocycle whereas cyt P460 uses a lysine residue to form one. In Nitrosomonas europaea, which expresses both HAO and cyt P460, these enzymes achieve the oxidation of NH2OH and were both originally reported to produce NO2-. Each can inspire means to effect controlled release of chemical energy.Spectroscopically studying the P460 cofactors of HAO is complicated by the 21 non-P460 heme cofactors, which obscure the active site. However, monoheme cyt P460 is more approachable biochemically and spectroscopically. Thus, we have used cyt P460 to study biological NH2OH oxidation. Under aerobic conditions substoichiometric production of NO2- was observed along with production of nitrous oxide (N2O). Under anaerobic conditions, however, N2O was the exclusive product of NH2OH oxidation. We have advanced our understanding of the mechanism of this enzyme and have showed that a key intermediate is a ferric nitrosyl that can dissociate the bound nitric oxide (NO) molecule and react with O2, thus producing NO2- abiotically. Because N2O was the true product of one P460 cofactor-containing enzyme, this prompted us to reinvestigate whether NO2- is enzymatically generated from HAO catalysis. Like cyt P460, we showed that HAO does not produce NO2- enzymatically, but unlike cyt P460, its final product is NO, establishing it as an intermediate of nitrification. More broadly, NO can be recognized as a molecule common to the primary metabolisms of all organisms involved in nitrogen "defixation".Delving deeper into cyt P460 yielded insights broadly applicable to controlled biochemical redox processes. Studies of an inactive cyt P460 from Nitrosomonas sp. AL212 showed that this enzyme was unable to oxidize NH2OH because it lacked a glutamate residue in its secondary coordination sphere that was present in the active N. europaea cyt P460 variant. Restoring the Glu residue imbued activity, revealing that a second-sphere base is Nature's key to controlled oxidation of NH2OH. A key lesson of bioinorganic chemistry is reinforced: the polypeptide matrix is an essential part of dictating function. Our work also exposed some key functional contributions of noncanonical heme-protein cross-links. The heme-Lys cross-link of cyt P460 enforces the relative position of the cofactor and second-sphere residues. Moreover, the cross-link prevents the dissociation of the axial histidine residue, which stops catalysis, emphasizing the importance of this unique post-translational modification.

Reversible C-C Bond Formation, Halide Abstraction, and Electromers in Complexes of Iron Containing Redox-Noninnocent Pyridine-imine Ligands.

The exploration of pyridine-imine (PI) iron complexes that exhibit redox noninnocence (RNI) led to several interesting discoveries. The reduction of (PI)FeX2 species afforded disproportionation products such as (dmpPI)2FeX (dmp = 2,6-Me2-C6H3, X = Cl, Br; 8-X) and (dippPI)2FeX (dipp = 2,6-iPr2-C6H3, X = Cl, Br; 9-X), which were independently prepared by reductions of (PI)FeX2 in the presence of PI. The crystal structure of 8-Br possessed an asymmetric unit with two distinct electromers, species with different electronic GSs: a low-spin (S = 1/2) configuration derived from an intermediate-spin S = 1 core antiferromagnetically (AF) coupled to an S = 1/2 PI ligand, and an S = 3/2 center resulting from a high-spin S = 2 core AF-coupled to an S = 1/2 PI ligand. Calculations were used to energetically compare plausible ground states. Polydentate diazepane-PI (DHPI) ligands were applied to the synthesis of monomeric dihalides (DHPI)FeX2 (X = Cl, 1-Cl2; X = Br, 1-Br2); reduction generated the highly distorted bioctahedral dimers (DHPA)2Fe2X2 ((3-X)2) containing a C-C bond formed from imine coupling; the monomers 1-X2 could be regenerated upon Ph3CX oxidation. Dihalides and their reduced counterparts were subjected to various alkyl halides and methyl methacrylate (MMA), generating polymers with little to no molecular weight control, indicative of simple radical-initiated polymerization.

A Nonheme Mononuclear {FeNO}7 Complex that Produces N2 O in the Absence of an Exogenous Reductant.

A new nonheme iron(II) complex, FeII (Me3 TACN)((OSiPh2 )2 O) (1), is reported. Reaction of 1 with NO(g) gives a stable mononitrosyl complex Fe(NO)(Me3 TACN)((OSiPh2 )2 O) (2), which was characterized by Mössbauer (δ=0.52 mm s-1 , |ΔEQ |=0.80 mm s-1 ), EPR (S=3/2), resonance Raman (RR) and Fe K-edge X-ray absorption spectroscopies. The data show that 2 is an {FeNO}7 complex with an S=3/2 spin ground state. The RR spectrum (λexc =458 nm) of 2 combined with isotopic labeling (15 N, 18 O) reveals ν(N-O)=1680 cm-1 , which is highly activated, and is a nearly identical match to that seen for the reactive mononitrosyl intermediate in the nonheme iron enzyme FDPnor (ν(NO)=1681 cm-1 ). Complex 2 reacts rapidly with H2 O in THF to produce the N-N coupled product N2 O, providing the first example of a mononuclear nonheme iron complex that is capable of converting NO to N2 O in the absence of an exogenous reductant.

The Heme-Lys Cross-Link in Cytochrome P460 Promotes Catalysis by Enforcing Secondary Coordination Sphere Architecture.

Cytochrome (cyt) P460 is a c-type monoheme enzyme found in ammonia-oxidizing bacteria (AOB) and methanotrophs; additionally, genes encoding it have been found in some pathogenic bacteria. Cyt P460 is defined by a unique post-translational modification to the heme macrocycle, where a lysine (Lys) residue covalently attaches to the 13' meso carbon of the porphyrin, modifying this heme macrocycle into the enzyme's eponymous P460 cofactor, similar to the cofactor found in the enzyme hydroxylamine oxidoreductase. This cross-link imbues the protein with unique spectroscopic properties, the most obvious of which is the enzyme's green color in solution. Cyt P460 from the AOB Nitrosomonas europaea is a homodimeric redox enzyme that produces nitrous oxide (N2O) from 2 equiv of hydroxylamine. Mutation of the Lys cross-link results in spectroscopic features that are more similar to those of standard cyt c' proteins and renders the enzyme catalytically incompetent for NH2OH oxidation. Recently, the necessity of a second-sphere glutamate (Glu) residue for redox catalysis was established; it plausibly serves as proton relay during the first oxidative half of the catalytic cycle. Herein, we report the first crystal structure of a cross-link deficient cyt P460. This structure shows that the positioning of the catalytically essential Glu changes by approximately 0.8 Å when compared to a cross-linked, catalytically competent cyt P460. It appears that the heme-Lys cross-link affects the relative position of the P460 cofactor with respect to the second-sphere Glu residue, therefore dictating the catalytic competency of the enzyme.

Structure, Spectroscopy, and Reactivity of a Mononuclear Copper Hydroxide Complex in Three Molecular Oxidation States.

Structural, spectroscopic, and reactivity studies are presented for an electron transfer series of copper hydroxide complexes supported by a tridentate redox-active ligand. Single crystal X-ray crystallography shows that the mononuclear [CuOH]1+ core is stabilized via intramolecular H-bonds between the H-donors of the ligand and the hydroxide anion when the ligand is in its trianionic form. This complex undergoes two reversible oxidation processes that produce two metastable "high-valent" CuOH species, which can be generated by addition of stoichiometric amounts of 1e- oxidants. These CuOH species are characterized by an array of spectroscopic techniques including UV-vis absorption, electron paramagnetic resonance (EPR), and X-ray absorption spectroscopies (XAS), which together indicate that all redox couples are ligand-localized. The reactivity of the complexes in their higher oxidation states toward substrates with modest O-H bond dissociation energies (e.g., 4-substitued-2,6-di-tert-butylphenols) indicates that these complexes act as 2H+/2e- oxidants, differing from the 1H+/1e- reactivity of well-studied [CuOH]2+ systems.

Electronic Structures and Reactivity Profiles of Aryl Nitrenoid-Bridged Dicopper Complexes.

Dicopper complexes templated by dinucleating, pacman dipyrrin ligand scaffolds (Mesdmx, tBudmx: dimethylxanthine-bridged, cofacial bis-dipyrrin) were synthesized by deprotonation/metalation with mesitylcopper (CuMes; Mes: mesityl) or by transmetalation with cuprous precursors from the corresponding deprotonated ligand. Neutral imide complexes (Rdmx)Cu2(µ2-NAr) (R: Mes, tBu; Ar: 4-MeOC6H4, 3,5-(F3C)2C6H3) were synthesized by treatment of the corresponding dicuprous complexes with aryl azides. While one-electron reduction of (Mesdmx)Cu2(µ2-N(C6H4OMe)) with potassium graphite initiates an intramolecular, benzylic C-H amination at room temperature, chemical reduction of (tBudmx)Cu2(µ2-NAr) leads to isolable [(tBudmx)Cu2(µ2-NAr)]- product salts. The electronic structures of the thermally robust [(tBudmx)Cu2(µ2-NAr)]0/- complexes were assessed by variable-temperature electron paramagnetic resonance spectroscopy, X-ray absorption spectroscopy (Cu L2,3/K-edge, N K-edge), optical spectroscopy, and DFT/CASSCF calculations. These data indicate that the formally Class IIIA mixed valence complexes of the type [(Rdmx)Cu2(µ2-NAr)]- feature significant NAr-localized spin following reduction from electronic population of the [Cu2(µ2-NAr)] π* manifold, contrasting previous methods for engendering iminyl character through chemical oxidation. The reactivity of the isolable imido and iminyl complexes are examined for prototypical radical-promoted reactivity (e.g., nitrene transfer and H-atom abstraction), where the divergent reactivity is rationalized by the relative degree of N-radical character afforded from different aryl substituents.

Scrutinizing "Ligand Bands" via Polarized Single-Crystal X-ray Absorption Spectra of Copper(I) and Copper(II) Bis-2,2'-bipyridine Species.

High-energy resolution fluorescence-detected Cu K-edge X-ray absorption spectroscopy (XAS) and single-crystal polarized XAS data are presented toward refining the assignments of bands assigned as excitations from Cu 1s to ligand-localized molecular orbitals. These have been previously dubbed "XAS-metal-ligand charge transfer" (XAS-MLCT) bands. Data are presented for a series of [Cu(xbpy)2]n+ complexes (xbpy = 2,2'-bipyridine (1n+), 4,4'-bisamino-2,2'-bipyridine (2n+), and 4,4'-dimethoxy-2,2'-bipyridine (3n+); n = 1 and 2). Dipolar dependencies of these "XAS-MLCT" bands in both Cu1+ and Cu2+ species lead to reassignment of these features as owing their intensities primarily to Cu 1s → Cu 4p excitations. The transition densities are Cu-localized, highlighting that XAS-MLCT features in Cu XAS spectra are not "charge transfer" transitions but rather quasi-atomic transitions. Although scrutiny of the acceptor orbitals supports assignment as Cu 1s → ligand π* transitions, it ultimately appears that while the ligand orbital energetics govern the positions of these bands the intensity is conferred through a small degree of metal 4p mixing into otherwise ligand-dominated acceptor molecular orbitals.

Heteroleptic Samarium(III) Chalcogenide Complexes: Opportunities for Giant Exchange Coupling in Bridging σ- and π-Radical Lanthanide Dichalcogenides.

The introduction of (N2)3-• radicals into multinuclear lanthanide molecular magnets raised hysteresis temperatures by stimulating strong exchange coupling between spin centers. Radical ligands with larger donor atoms could promote more efficient magnetic coupling between lanthanides to provide superior magnetic properties. Here, we show that heavy chalcogens (S, Se, Te) are primed to fulfill these criteria. The moderately reducing Sm(II) complex, [Sm(N††)2], where N†† is the bulky bis(triisopropylsilyl)amide ligand, can be oxidized (i) by diphenyldichalcogenides E2Ph2 (E = S, Se, Te) to form the mononuclear series [Sm(N††)2(EPh)] (E = S, 1-S; Se, 1-Se, Te, 1-Te); (ii) S8 or Se8 to give dinuclear [{Sm(N††)2}2(µ-η2:η2-E2)] (E = S, 2-S2; Se, 2-Se2); or (iii) with Te═PEt3 to yield [{Sm(N††)2}(µ-Te)] (3). These complexes have been characterized by single crystal X-ray diffraction, multinuclear NMR, FTIR, and electronic spectroscopy; the steric bulk of N†† dictates the formation of mononuclear complexes with chalcogenate ligands and dinuclear species with the chalcogenides. The Lα1 fluorescence-detected X-ray absorption spectra at the Sm L3-edge yielded resolved pre-edge and white-line peaks for 1-S and 2-E2, which served to calibrate our computational protocol in the successful reproduction of the spectral features. This method was employed to elucidate the ground state electronic structures for proposed oxidized and reduced variants of 2-E2. Reactivity is ligand-based, forming species with bridging superchalcogenide (E2)-• and subchalcogenide (E2)3-• radical ligands. The extraordinarily large exchange couplings provided by these dichalcogenide radicals reveal their suitability as potential successors to the benchmark (N2)3-• complexes in molecular magnets.

[(MeCN)Ni(CF3)3]- and [Ni(CF3)4]2-: Foundations toward the Development of Trifluoromethylations at Unsupported Nickel.

Nickel anions [(MeCN)Ni(CF3)3]- and [Ni(CF3)4]2- were prepared by the formal addition of 3 and 4 equiv, respectively, of AgCF3 to [(dme)NiBr2] in the presence of the [PPh4]+ counterion. Detailed insights into the electronic properties of these new compounds were obtained through the use of density functional theory (DFT) calculations, spectroscopy-oriented configuration interaction (SORCI) calculations, X-ray absorption spectroscopy, and cyclic voltammetry. The data collectively show that trifluoromethyl complexes of nickel, even in the most common oxidation state of nickel(II), are highly covalent systems whereby a hole is distributed on the trifluoromethyl ligands, surprisingly rendering the metal to a physically more reduced state. In the cases of [(MeCN)Ni(CF3)3]- and [Ni(CF3)4]2-, these complexes are better physically described as d9 metal complexes. [(MeCN)Ni(CF3)3]- is electrophilic and reacts with other nucleophiles such as phenoxide to yield the unsupported [(PhO)Ni(CF3)3]2- salt, revealing the broader potential of [(MeCN)Ni(CF3)3]- in the development of "ligandless" trifluoromethylations at nickel. Proof-in-principle experiments show that the reaction of [(MeCN)Ni(CF3)3]- with an aryl iodonium salt yields trifluoromethylated arene, presumably via a high-valent, unsupported, and formal organonickel(IV) intermediate. Evidence of the feasibility of such intermediates is provided with the structurally characterized [PPh4]2[Ni(CF3)4(SO4)], which was derived through the two-electron oxidation of [Ni(CF3)4]2-.