A Review of Electrocatalytic Reduction of Dinitrogen to Ammonia under Ambient Conditions

The production of ammonia (NH₃) from molecular dinitrogen (N₂) under mild conditions is one of the most attractive topics in the field of chemistry. Electrochemical reduction of N₂ is promising for achieving clean and sustainable NH₃ production with lower energy consumption using renewable energy sources. To date, emerging electrocatalysts for the electrochemical reduction of N₂ to NH₃ at room temperature and atmospheric pressure remain largely underexplored. The major challenge is to achieve both high catalytic activity and high selectivity. Here, the recent progress on the electrochemical nitrogen reduction reaction (NRR) at ambient temperature and pressure from both theoretical and experimental aspects is summarized, aiming at extracting instructive perceptions for future NRR research activities. The prevailing theories and mechanisms for NRR as well as computational screening of promising materials are presented. State‐of‐the‐art heterogeneous electrocatalysts as well as rational design of the whole electrochemical systems for NRR are involved. Importantly, promising strategies to enhance the activity, selectivity, efficiency, and stability of electrocatalysts toward NRR are proposed. Moreover, ammonia determination methods are compared and problems relating to possible ammonia contamination of the system are mentioned so as to shed fresh light on possible standard protocols for NRR measurements.     

Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations

In this study, the interaction between human serum albumin (HSA) and a copper complex of carmoisine dye; [Cu(carmoisine)₂(H₂O)₂], was studied in vitro using multi‐spectroscopic methods. It was found that the intrinsic fluorescence of HSA was quenched by the addition of the [Cu(carmoisine)₂(H₂O)₂] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine)₂(H₂O)₂]–HSA complex. The binding constant was about 10⁴ M^?1 at room temperature. The values of the calculated thermodynamic parameters (ΔH < 0 and ΔS > 0) suggested that both hydrogen bonds and the hydrophobic interactions were involved in the binding process. The site marker competitive experiments revealed that the binding of [Cu(carmoisine)₂(H₂O)₂] to HSA primarily occurred in subdomain IIIA (site II) of HSA. The results of circular dichroism (CD) and UV–vis spectroscopy showed that the micro‐environment of amino acid residues and the conformation of HSA were changed after addition of the [Cu(carmoisine)₂(H₂O)₂] complex. Finally, the binding of the [Cu(carmoisine)₂(H₂O)₂] complex to HSA was modelled by a molecular docking method. Excellent agreement was obtained between the experimental and theoretical results with respect to the binding forces and binding constant.     

Quantum chemistry as a tool in bioenergetics

Recent developments of quantum chemical methods have made it possible to tackle crucial questions in bioenergetics. The most important systems, cytochrome c oxidase in cellular respiration and photosystem II (PSII) in photosynthesis will here be used as examples to illustrate the power of the quantum chemical tools. One main contribution from quantum chemistry is to put mechanistic suggestions onto an energy scale. Accordingly, free energy profiles can be constructed both for reduction of molecular oxygen in cytochrome c oxidase and water oxidation in PSII, including O-O bond cleavage and formation, and also proton pumping in cytochrome c oxidase. For the construction of the energy diagrams, the computational results sometimes have to be combined with experimental information, such as reduction potentials and rate constants for individual steps in the reactions.     

Quantitative analysis of FRET assay in biology—new developments in protein interaction affinity and protease kinetics determinations in the SUMOylation cascade

F(o)rster resonance energy transfer (FRET) techniques have been widely used in biological studies in vitro and in vivo and are powerful tools for elucidating protein interactions in many regulatory cas...     

A hexanuclear iron(III) complex [Fe6O2(OH)2(PhCOO)10(hedmp)2]·3CH3CN assembled from 2-hydroxyethyl-3,5-dimethyl pyrazole

In order to assemble polynuclear iron(III) complexes, the coordination chemistry of the 2-hydroxyethyl-3,5-dimethylpyrazole (hedmp-H) ligand has been investigated. Reaction of hedmp-H with trinuclear iron carboxylate precursor [Fe₃O(PhCOO)₆(H₂O)₃]Cl in acetonitrile yielded the hexanuclear Fe(III) complex [Fe₆O₂(OH)₂(PhCOO)₁₀(hedmp)₂]·3CH₃CN (1). This aggregate has been characterized by employing various analytical techniques, spectroscopic studies and single crystal X-ray diffraction. Detailed magnetic susceptibility measurements revealed that 1 displays an S_T = 5 ground state.     

DNA-binding and photocleavage studies of [Ru(phen)2(NMIP)]

A novel ligand 2′-(2″-nitro-3″,4″-methylenedioxyphenyl)imidazo[4′,5′-f][1,10]-phenanthroline (NMIP) and its complex [Ru(phen)₂(NMIP)]²⁺ have been synthesized and characterized by mass spectroscopy, ¹H NMR and cyclic voltammetry. Binding of the complex with calf thymus DNA (CT DNA) has been investigated by spectroscopic methods, viscosity and electrophoresis measurements. The experimental results indicate that [Ru(phen)₂(NMIP)]²⁺ binds to DNA via partial intercalative mode and the individual enantiomers of it bind to DNA in different rates. [Ru(phen)₂(NMIP)]²⁺ has also been found to promote cleavage of plasmid pBR 322 DNA from the supercoiled Form I to the open circular Form II upon irradiation.     

Structures of the intermediates in the catalytic cycle of mitochondrial cytochrome c oxidase

Cytochrome c oxidase is the terminal complex of the respiratory chains in the mitochondria of nearly all eukaryotes. It catalyzes the reduction of molecular O₂ to water using electrons from the respiratory chain, delivered via cytochrome c on the external surface of the inner mitochondrial membrane. The protons required for water formation are taken from the matrix side of the membrane, making catalysis vectorial. This vectorial feature is further enhanced by the fact that the redox catalysis is coupled to the translocation of protons from the inside to the outside of the inner mitochondrial membrane. We are dealing with a molecular machine that converts redox free energy into a protonmotive force (pmf). Here, we review the current extensive knowledge of the structural changes in the active heme?copper site that accompany catalysis, based on a large variety of time-resolved spectroscopic experiments, X-ray and cryoEM structures, and advanced computational chemistry.     

New Guaiane-Type Sesquiterpene and Norsesquiterpene from Alisma plantago-aquatica and Their Xanthine Oxidase Inhibitory Activity

A new sesquiterpene ( 1 ) and a new norsesquiterpene ( 2 ) belonging guaiane-type skeleton together with six known compounds ( 3 – 8 ) were isolated from the rhizomes of Alisma plantago-aquatica. Their structures were determined by HR-ESI-MS, 1D and 2D NMR spectroscopic methods. Absolute configurations of new compounds were established by experimental and TD-DFT computational ECD spectra. Compounds 1 – 8 exhibited xanthine oxidase inhibitory activity with their IC₅₀ values in range of 9.4–66.7 μM. The sesquiterpenoids 1 – 5 displayed the inhibitory activity and hence they could be potential xanthine oxidase inhibitors from A. plantago-aquatica.     

Coupled reactions for the determination of analytes and enzymes based on the use of luminescence

Immobilized enzymes are widely used in the clinical laboratory in the assay of several analytes and enzymes. The use of immobilized enzymes makes these reagents recoverable and re-usable, and in most cases increases their stability and catalytic activity. In conjunction with bioluminescent enzymes (firefly and bacterial luciferases) and chemiluminescent catalyst (peroxidase) we set up high-sensitive flow methods based on the use of nylon tube coil or epoxy methacrylate column as solid support. All the NAD(P)/NAD(P)H-dependent dehydrogenases (bacterial luciferase), ATP-dependent enzymes (firefly luciferase) and oxidases producing H₂O₂ (peroxidase) can be immobilized and a large variety of analytes have been sensitively measured. As an alternative format we also reported a dry chemistry method in which all the enzymes, substrates and cofactors are ready to use, supported on dry cellulose disks. Methodological problems such as flow conditions, stability, pH, ionic strength and analytical performances are also reported.     

Allosteric modulation of adenosine receptors

Allosteric modulators for adenosine receptors may have potential therapeutic advantage over orthosteric ligands. Allosteric enhancers at the adenosine A₁ receptor have been linked to antiarrhythmic and antilipolytic activity. They may also have therapeutic potential as analgesics and neuroprotective agents. A₃ allosteric enhancers are postulated to be useful against ischemic conditions or as antitumor agents. In this review, we address recent developments regarding the medicinal chemistry of such compounds. Most efforts have been and are directed toward adenosine A₁ and A₃ receptors, whereas limited or no information is available for A_2A and A_2B receptors. We also discuss some findings, mostly receptor mutation studies, regarding localization of the allosteric binding sites on the receptors.     

Studies on the Interaction of [SnMe2Cl2(bu2bpy)] Complex with ct-DNA Using Multispectroscopic,Atomic Force Microscopy (AFM) and Molecular Docking

The interaction of SnMe₂Cl₂(bu₂bpy)complex with calf thymus DNA (ct-DNA) has been explored following, using spectroscopic methods, viscosity measurements, Atomic force microscopy, Thermal denaturation and Molecular docking. It was found that Sn(IV) complex could bind with DNA via intercalation mode as evidenced by hyperchromism and bathochromic in UV–Vis spectrum; these spectral characteristics suggest that the Sn(IV) complex interacts with DNA most likely through a mode that involves a stacking interaction between the aromatic chromophore and the base pairs of DNA. In addition, the fluorescence emission spectra of intercalated methylene blue (MB) with increasing concentrations of SnMe₂Cl₂(bu₂bpy) represented a significant increase of MB intensity as to release MB from MB-DNA system. Positive values of ΔH and ΔS imply that the complex is bound to ct-DNA mainly via the hydrophobic attraction. Large complexes contain the DNA chains with an average size of 859?nm were observed by using AFM for Sn(IV) Complex–DNA. The Fourier transform infrared study showed a major interaction of Sn(IV) complex with G-C and A-T base pairs and a minor perturbation of the backbone PO₂ group. Addition of the Sn(IV)complex results in a noticeable rise in the Tm of DNA. In addition, the results of viscosity measurements suggest that SnMe₂Cl₂(bu₂bpy) complex may bind with the classical intercalative mode. From spectroscopic and hydrodynamic studies, it has been found that Sn(IV)complex interacts with DNA by intercalation mode. Optimized docked model of DNA–complex mixture confirmed the experimental results.     

Structural variation within uranium heterocyclic carboxylates: Solid and solution states studies

The solution chemistry and solid-state structures of two new uranium^VI metal-organic compounds, (tataH)₂[(UO₂)₂(pdtc)₂(μ-OH)₂]·2H₂O (1) and (AcrH)₂[(UO₂)(pydc)₂] (2), [where tata = 1,3,5-triazine-2,4,6-triamine, Acr = acridine, pydc = pyridine-2,6-dicarboxylate and pdtc = pyridine-2,6-bis(monothiocarboxylate)] have been investigated. These compounds were obtained via proton-transfer methodology by reacting UO₂²⁺ with the preformed proton-transfer systems (tataH)₂(pdtc) and (AcrH)₂(pydc), respectively, in aqueous solution, after evaporation of the solvent. Our results show that noncovalent interactions such as hydrogen bonds, sulfur···sulfur, and π···π interactions, when acting cooperatively, are driving forces for the selection of different structures. The protonation constants of Acr, tata, pdtcH₂, and pydcH₂, the building blocks of the proton-transfer systems (tataH)₂(pdtc) and (AcrH)₂(pydc), and the stability constants of these systems were determined by potentiometric studies in a dioxane/H₂O (1:1 v/v) mixture. The stoichiometry and the formation stability constants of complexes formed on reacting pydcH₂/Acr or pdtcH₂/tata 1:1 molar mixtures with the UO₂²⁺ ion in dioxane/H₂O (1:1 v/v) were investigated by potentiometric pH titration methods. The stoichiometries of the complex species formed in solution were compared with those observed for the crystalline metal ion complexes 1 and 2.     

Synthesis, crystal structure, characterization of zinc(II), cadmium(II) complexes with 3-thiophene aldehyde thiosemicarbazone (3TTSCH). Biological activities of 3TTSCH and its complexes

The reaction of zinc(II) chloride, cadmium(II) chloride and bromide with 3-thiophene aldehyde thiosemicarbazone leads to the formation of a series of new complexes. They have been characterized by spectroscopic studies: infrared, ¹H NMR, and electronic spectra. The crystal structures of the compound [ZnCl₂(3TTSCH)₂] and [CdBr₂(3TTSCH)₂] have been determined by X-ray diffraction methods. For the complexes [ZnCl₂(3TTSCH)₂] and [CdBr₂(3TTSCH)₂], the central ion is coordinated through the sulfur, and for the complexes [CdCl₂(3TTSCH)], [CdBr₂(3TTSCH)] the ion is coordinated through the sulfur as well as azomethine nitrogen atom of the thiosemicarbazone. In addition, fungistatic and bacteriostatic activities of both ligand and complexes have been evaluated. Cadmium(II) complexes have shown the most significant activities.     

Preparation and structural characterization of group 1 metal complexes containing a chelating biphenolato phosphine ligand

The coordination chemistry of a potentially tridentate, dianionic biphenolato phosphine ligand with respect to group 1 metals is described. Deprotonation of bis-(3,5-di-tert-butyl-2-hydroxyphenyl)phenylphosphine (H₂[OPO]) with two equivalents of n-BuLi, NaH, or KH in dimethoxyethane (DME) solutions produces the corresponding dinuclear alkali metal complexes [OPO]M₂(DME)₂ (M = Li, Na, K). The X-ray structure of [OPO]Li₂(DME)₂ reveals that the two lithium atoms are bridged by both phenolato oxygen donors with only one lithium being coordinated to the phosphorus donor. Consistently, variable-temperature ³¹P{¹H} and ⁷Li{¹H} NMR spectroscopic studies elucidate the coordination of the phosphorus donor in [OPO]Li₂(DME)₂ to one of the lithium atoms in solution. Interestingly, an X-ray diffraction study of the potassium complex indicates a dimeric structure with S₂ symmetry for this species in which the four potassium atoms are bridged by both phosphorus and oxygen donors of the biphenolato phosphine ligands. These alkali metal complexes are active initiators for catalytic ring-opening polymerization of ε-caprolactone.     

Urea’s Effect on the Ribonuclease A Catalytic Efficiency: A Kinetic, 1H NMR and Molecular Orbital Study

Understanding of protein–urea interactions is one of the greatest challenges to modern structural protein chemistry. Based in enzyme kinetics experiments and ¹H NMR spectroscopic analysis we proposed that urea, at low concentrations, directly interacts with the protonated histidines of the active center of RNase A, following a simple model of competitive inhibition. These results were supported by theoretical analysis based on the frontier molecular orbital theory and suggest that urea might establish a favorable interaction with the cationic amino acids. Our experimental evidence and theoretical analysis indicate that the initials steps of the molecular mechanism of Urea–RNase A interaction passes through the establishment of a three center four electron adduct. Also, our results would explain the observed disruption of the ¹H NMR signals corresponding to H12 and H119 (involved in catalysis) of the RNase A studied in the presence of urea. Our interaction model of urea–amino acids (cationic) can be extended to explain the inactivation of other enzymes with cationic amino acids at the active site.     

On the interaction of compounds of chromium(VI) with hydrogen peroxide. A study of chromium(VI) and (V) peroxides in the acid-basic pH range

A computational study of chromium(VI) and (V) peroxides, which exhibit important genotoxic and mutagenic activity, is reported. Energies and equilibrium geometries for [Cr^VI(O)(O₂)₂(OH)]⁻, [Cr^VI(O)(O₂)₂(OH₂)], [Cr^VI(O)(O₂)₂(py)], [Cr^VI(OH)(O₂)₂(OH₂)]⁺, [Cr^V(O)(O₂)₂(OH₂)]⁻ and species were calculated using molecular mechanics calculations (MMFF94 and MM⁺), quantum calculations with semi-empirical methods (RHF and UHF/PM3) and density functional theory (pBP86/DN* or pBP/DN* and B3LYP/6-31G(d). Equilibrium geometries for the compounds [Cr^V(O₂)₃(OH)]²⁻ and [Cr^V(O₂)₄]³⁻ were determined by molecular mechanics. Vibrational frequencies, standard thermodynamic quantities and electronic spectra were calculated using B3LYP/6-31G(d). The structural relationship between all these species and an explanation of the formation of peroxo species in the acid-basic pH range are given. An experimental study of peroxo species in basic medium was also performed (synthesis, X-ray powder diffraction patterns and infrared spectra of the peroxo complexes isolated) but did not confirm the existence of a tri-peroxo complex in the solid phase.     

Complex formation and characterization of MgCl2/2-(2-ethylhexyloxy)ethanol adduct

Complex formation of MgCl₂ with 2-(2-ethylhexyloxy)ethanol was studied by IR and NMR spectroscopic methods and molecular modeling to determine the binding mode of the alcohol to MgCl₂. According to both experimental and theoretical studies, during the reaction of the alcohol and MgCl₂, two alcohol molecules form an adduct with MgCl₂ through the oxygen atoms of the alcohol and ether groups, giving rise to a chelated structure. Crystallization of the MgCl₂/2-(2-ethylhexyloxy)ethanol complex was attempted by various methods. Toluene was used as solvent in the dissolution of MgCl₂ in alcohol, and heptane was used to adjust the solubility of MgCl₂ during the crystallization. Crystals piled up as thin plates. Single-crystal X-ray structure analysis revealed a chelated structure formed through the oxygen atoms of the ether and alcohol groups. Two water molecules are also bound to the magnesium, as seen in the IR spectrum of the crystals as well.     

Revisiting the optical properties of the FMO protein

We review the optical properties of the FMO complex as found by spectroscopic studies of the Q _y band over the last two decades. This article emphasizes the different methods used, both experimental and theoretical, to elucidate the excitonic structure and dynamics of this pigment–protein complex.