Redox Communication within Multinuclear Iron–Sulfur Complexes Related to Electronic Interplay in the Active Site of [FeFe]Hydrogenase

The one‐electron oxidations of a Fe₂ complex lead to the formation of a persistent metal‐stabilized thiyl radical Fe₂ species, mixed‐valent Fe₄, and Fe₈ complexes. The unpaired spin in the Fe₂ radical species delocalizes over the Fe₂ and the aromatic dithiolate, mostly on the terminal sulfur. The subsequent dimerization of the singly oxidized Fe₂ to the Fe₄ retains the partial thiyl radical character. For an analogue with less steric hindrance, the π–π stacking interaction between the dithiolato aromatic rings induces generation of the Fe₈, in which process electronic structures of the species are modulated through reducing the thiyl radical to the thiolate. Electronic reorganization repeats when the Fe₈ is converted to Fe₄. Electronic interplay in the complexes decreases the energy gap of frontier MOs and buffers electronic impacts upon redox events. Easier accessible redox potentials and increased stability of the species are facilitated. The results demonstrate that electronic versatility of the benzenedithiolate exerts pronounced influences on electronic and coordination structure of the metal complexes.     

An Objective Alternative to IUPAC's Approach To Assign Oxidation States

The IUPAC has recently clarified the term oxidation state (OS), and provided algorithms for its determination based on the ionic approximation (IA) of the bonds supported by atomic electronegativities (EN). Unfortunately, there are a number of exceptions and ambiguities in IUPAC's algorithms when it comes to practical applications. Our comprehensive study reveals the critical role of the chemical environment on establishing the OS, which cannot always be properly predicted using fix atomic EN values. By identifying what we define here as subsystems of enhanced stability within the molecular system, the OS can be safely assigned in many cases without invoking exceptions. New insights about the effect of local aromaticity upon OS are revealed. Moreover, we prove that there are intrinsic limitations of the IA that cannot be overcome. In this context, the effective oxidation state (EOS) analysis arises as a robust and general scheme to derive an OS without any external guidance.     

Controlled Anchoring of (Phenylureido)sulfonamide-Based Receptor Moieties: An Impact of Binding Site Multiplication on Complexation Properties

The repetition of urea-based binding units within the receptor structure does not only lead to monomer properties multiplication. As confirmed by spectroscopic studies, UV-Vis and ¹H-NMR in classical or competitive titration mode, the attachment to a carrier allocates the active moieties to mutual positions predetermining the function of the whole receptor molecule. Bivalent receptors form self-aggregates. Dendritic receptors with low dihydrogen phosphate loadings offer a cooperative complexation mode associated with a positive dendritic effect. In higher dihydrogen phosphate concentrations, the dendritic branches act independently and the binding mode changes to 1:1 anion: complexation site. Despite the anchoring, the dendritic receptors retain the superior efficiency and selectivity of a monomer, paving the way to recyclable receptors, desirable for economic and ecological reasons.     

A Promising Approach for Controlling the Second Coordination Sphere of Biomimetic Metal Complexes: Encapsulation in a Dynamic Hydrogen-Bonded Capsule

The design of biomimetic models of metalloenzymes needs to take into account many factors and is therefore a challenging task. We propose in this work an original strategy to control the second coordination sphere of a metal centre and its distal environment. A biomimetic complex, reproducing the first coordination sphere, is encapsulated in a self-assembled hydrogen-bonded capsule. The cationic complex is co-encapsulated with its counter-anion or with solvent molecules. The capsule is dynamic, allowing a fast in/out exchange of the co-encapsulated species. It also provides both a hydrogen-bonding site in the second coordination sphere and a source of proton as it can be deprotonated in the presence of the complex, providing a globally neutral host-guest assembly. This simple and broad scope strategy is unprecedented in biomimetic studies. The approach appears to be a very promising method for the stabilisation of reactive species and for the study of their reactivity.     

Hemoglobin as a nitrite anhydrase: modeling methemoglobin-mediated N2O3 formation

Nitrite has recently been recognized as a storage form of NO in blood and as playing a key role in hypoxic vasodilation. The nitrite ion is readily reduced to NO by hemoglobin in red blood cells, which, as it happens, also presents a conundrum. Given NO’s enormous affinity for ferrous heme, a key question concerns how it escapes capture by hemoglobin as it diffuses out of the red cells and to the endothelium, where vasodilation takes place. Dinitrogen trioxide (N₂O₃) has been proposed as a vehicle that transports NO to the endothelium, where it dissociates to NO and NO₂. Although N₂O₃ formation might be readily explained by the reaction Hb‐Fe³⁺+NO₂^?+NO?Hb‐Fe²⁺+N₂O₃, the exact manner in which methemoglobin (Hb‐Fe³⁺), nitrite and NO interact with one another is unclear. Both an “Hb‐Fe³⁺‐NO₂^?+NO” pathway and an “Hb‐Fe³⁺‐NO+NO₂^?” pathway have been proposed. Neither pathway has been established experimentally. Nor has there been any attempt until now to theoretically model N₂O₃ formation, the so‐called nitrite anhydrase reaction. Both pathways have been examined here in a detailed density functional theory (DFT, B3LYP/TZP) study and both have been found to be feasible based on energetics criteria. Modeling the “Hb‐Fe³⁺‐NO₂^?+NO” pathway proved complex. Not only are multiple linkage‐isomeric (N‐ and O‐coordinated) structures conceivable for methemoglobin–nitrite, multiple isomeric forms are also possible for N₂O₃ (the lowest‐energy state has an N? N‐bonded nitronitrosyl structure, O₂N? NO). We considered multiple spin states of methemoglobin–nitrite as well as ferromagnetic and antiferromagnetic coupling of the Fe³⁺ and NO spins. Together, the isomerism and spin variables result in a diabolically complex combinatorial space of reaction pathways. Fortunately, transition states could be successfully calculated for the vast majority of these reaction channels, both M_S=0 and M_S=1. For a six‐coordinate Fe³⁺‐O‐nitrito starting geometry, which is plausible for methemoglobin–nitrite, we found that N₂O₃ formation entails barriers of about 17–20 kcal mol^?1, which is reasonable for a physiologically relevant reaction. For the “Hb‐Fe³⁺‐NO+NO₂^?” pathway, which was also found to be energetically reasonable, our calculations indicate a two‐step mechanism. The first step involves transfer of an electron from NO₂^? to the Fe³⁺–heme–NO center ({FeNO}⁶) , resulting in formation of nitrogen dioxide and an Fe²⁺–heme–NO center ({FeNO}⁷). Subsequent formation of N₂O₃ entails a barrier of only 8.1 kcal mol^?1. From an energetics point of view, the nitrite anhydrase reaction thus is a reasonable proposition. Although it is tempting to interpret our results as favoring the “{FeNO}⁶+NO₂^?” pathway over the “Fe³⁺‐nitrite+NO” pathway, both pathways should be considered energetically reasonable for a biological reaction and it seems inadvisable to favor a unique reaction channel based solely on quantum chemical modeling.     

Binding of a Ruthenium Complex to a Thioether Ligand Embedded in a Negatively Charged Lipid Bilayer: A Two‐Step Mechanism

The interaction between the ruthenium polypyridyl complex [Ru(terpy)(dcbpy)(H₂O)]²⁺ (terpy=2,2′;6′,2“‐terpyridine, dcbpy=6,6′‐dichloro‐2,2′‐bipyridine) and phospholipid membranes containing either thioether ligands or cholesterol were investigated using UV–visible spectroscopy, Langmuir–Blodgett monolayer surface pressure measurements, and isothermal titration calorimety (ITC). When embedded in a membrane, the thioether ligand coordinated to the dicationic metal complex only when the phospholipids of the membrane were negatively charged, that is, in the presence of attractive electrostatic interaction. In such a case coordination is much faster than in homogeneous conditions. A two‐step model for the coordination of the metal complex to the membrane‐embedded sulfur ligand is proposed, in which adsorption of the complex to the negative surface of the monolayers or bilayers occurs within minutes, whereas formation of the coordination bond between the surface‐bound metal complex and ligand takes hours. Finally, adsorption of the aqua complex to the membrane is driven by entropy. It does not involve insertion of the metal complex into the hydrophobic lipid layer, but rather simple electrostatic adsorption at the water–bilayer interface.     

Characterization of a Multicomponent Lithium Lithiate from a Combined X‐Ray Diffraction,NMR Spectroscopy,and Computational Approach

An unusual lithium lithiate [Li(diglyme)₂][(diglyme)Li₂(C₄H₃S)₃], made up from three carbanions, two lithium cations, and a single donor base molecule in the anion and a single lithium cation, coordinated by two donor base molecules, is investigated in a combined study including X‐ray diffraction, NMR spectroscopy and computational approaches in solution and the solid state. While the multicomponent lithiate is the only species present in the solid state, solution NMR spectroscopy and computational methods were employed to identify a second species in solution. The dimer [(diglyme)Li(C₄H₃S)]₂ coexists with the lithiate in solution in a 1:1 ratio, the more the higher the polarity of the solvent is. Only the combination of this multitude of methods provides a firm picture of the whole.     

Electrochemical Formation of Fe(IV)=O Derived from H2O2 on a Hematite Electrode as an Active Catalytic Site for Selective Hydrocarbon Oxidation Reactions

The high-valence iron species (Fe(IV)=O) in the cytochrome P450 enzyme superfamily is generated via the activation of O₂, and serves as the active center of selective hydrocarbon oxidation reactions. Furthermore, P450 can employ an alternate route to produce Fe(IV)=O, even from H₂O₂ without O₂ activation. Meanwhile, Fe(IV)=O has recently been revealed to be the reactive intermediate during H₂O oxidation to O₂ on hematite electrodes. Herein, we demonstrated the generation of Fe(IV)=O on hematite electrodes during the electrochemical oxidative decomposition of H₂O₂ using in situ UV-visible absorption spectra. The generation of Fe(IV)=O on hematite electrodes from H₂O₂ exhibited 100 mV lower overpotential than that from H₂O. This is because H₂O₂ serves not only as the oxygen source of Fe(IV)=O, but also as the additional oxidant. Finally, we confirmed that the Fe(IV)=O generated on hematite electrodes can serve as the catalytic site for styrene epoxidation reactions.     

ChemInform Abstract: DFT Analysis of Cubane‐Type FeIr3S4 Clusters. Dinitrogen Binding and Activation at the Tetrahedral Fe Site.

ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.     

Revealing the Bonding Pattern from the Molecular Electron Density Using Single Exponential Decay Detector: An Orbital‐Free Alternative to the Electron Localization Function

We introduce a new tool (single exponential decay detector: SEDD) to extract information about bonding and localization in atoms, molecules, or molecular assemblies. The practical evaluation of SEDD does not require any explicit information about the orbitals. The only quantity needed is the electron density (calculated or experimental) and its derivatives up to the second order.     

The Influence of the Framework: An Anion‐Binding Study Using Fused [n]Polynorbornanes

A series of bis‐thiourea‐functionalized [n]polynorbornane hosts ( 1 – 6 ) with increasing size were synthesized and their anion‐binding properties were evaluated by using ¹H NMR spectroscopic titration and Job’s plot analysis. The larger bis‐thiourea‐[3]polynorbornane scaffolds 4 and 5 bound acetate in a 1:1 (cooperative) arrangement, whereas the corresponding smaller norbornane host 2 , identical in preorganization, bound acetate in a 1:2 (independent) arrangement. In contrast, the size of the framework had no influence on the binding of dihydrogenphosphate. These results clearly highlight the subtle influence that the framework itself can have on host–guest interactions.     

An Artificial Enzyme Made by Covalent Grafting of an FeII Complex into β‐Lactoglobulin: Molecular Chemistry,Oxidation Catalysis,and Reaction‐Intermediate Monitoring in a Protein

An artificial metalloenzyme based on the covalent grafting of a nonheme Fe^II polyazadentate complex into bovine β‐lactoglobulin has been prepared and characterized by using various spectroscopic techniques. Attachment of the Fe^II catalyst to the protein scaffold is shown to occur specifically at Cys121. In addition, spectrophotometric titration with cyanide ions based on the spin‐state conversion of the initial high spin (S=2) Fe^II complex into a low spin (S=0) one allows qualitative and quantitative characterization of the metal center’s first coordination sphere. This biohybrid catalyst activates hydrogen peroxide to oxidize thioanisole into phenylmethylsulfoxide as the sole product with an enantiomeric excess of up to 20 %. Investigation of the reaction between the biohybrid system and H₂O₂ reveals the generation of a high spin (S=5/2) Fe^III(η²‐O₂) intermediate, which is proposed to be responsible for the catalytic sulfoxidation of the substrate.     

A Bioorthogonal Approach for the Preparation of a Titanium‐Binding Insulin‐like Growth‐Factor‐1 Derivative by Using Tyrosinase

The generation of metal surfaces with biological properties, such as cell‐growth‐enhancing and differentiation‐inducing abilities, could be potentially exciting for the development of functional materials for use in humans, including artificial dental implants and joint replacements. However, currently the immobilization of proteins on the surfaces of the metals are limited. In this study, we have used a mussel‐inspired bioorthogonal approach to design a 3,4‐hydroxyphenalyalanine‐containing recombinant insulin‐like growth‐factor‐1 using a combination of recombinant DNA technology and tyrosinase treatment for the surface modification of titanium. The modified growth factor prepared in this study exhibited strong binding affinity to titanium, and significantly enhanced the growth of NIH3T3 cells on the surface of titanium.     

Computational Ligand Design for the Reductive Elimination of ArCF3 from a Small Bite Angle PdII Complex: Remarkable Effect of a Perfluoroalkyl Phosphine

To date only three ligands are known to trigger the challenging reductive elimination of ArCF₃ from Pd^II. We report the computational design of a bidentate trifluoromethylphosphine ligand that although exhibiting a generally ineffective small bite angle is predicted to give facile reductive elimination. Our experimental verification gave quantitative formation of ArCF₃ at 80 °C within 2 h. This highlights the distinct effect of P‐CF₃ in organometallic reactivity and constitutes a proof‐of‐principle study of computational reactivity design.