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The achievement of targeted properties in spin crossover (SCO) materials is complicated by often unpredictable cooperative interactions in the solid state. Herein, we report a dinuclear Fe(II) triple helicate 1, which is a rare example of a SCO material possessing two distinct magnetic behaviors that depend upon the thermal scan rate. Desolvated 1 was seen to undergo spin transition (ST) which was complete following slow cooling (1 K min-1), but incomplete ST (corresponding to 50% conversion) on fast cooling (10 K min-1). The incomplete ST observed in the latter case was accompanied by a higher temperature onset of ST, differing from TIESST (Temperature-Induced Excited Spin-State Trapping) materials. The two SCO pathways have been shown to arise from the interconversion between two structural phases (a and b), with both phases having associated high spin (HS) and low spin (LS) states. SCXRD (Single Crystal X-ray Diffraction) experiments using controlled cooling rates and a synchrotron light source enabled short collection times (2-3 minutes per dataset) which has enabled the identification of a mechanism by which the slow-cooled material may fully relax. In contrast, fast-cooled materials exhibit disordered arrangements of multiple structural phases, which has in turn revealed that the [HS-LS] ↔ [LS-HS] equilibria are controllable in the solid by varying the scan rate. Such behavior has been previously observed in solution studies, but its control in solids has not been reported up to now. This study demonstrates how intermolecular cooperativity can allow multiple distinct magnetic behaviors, and provides some insight into how [HS-LS] ↔ [LS-HS] equilibria can be controlled in the solid state, which may assist in the design of next-generation logic and signaling devices.

Application of iron (Fe)- and silica (Si)-enhanced biochar compound fertilisers (BCF) stimulates rice yield by increasing plant uptake of mineral nutrients. With alterations of the nutrient status in roots, element homeostasis (e.g., Fe) in the biochar-treated rice root was related to the formation of biominerals on the plaque layer and in the cortex of roots. However, the in situ characteristics of formed biominerals at the micron and sub-micron scale remain unknown. In this study, rice seedlings (Oryza sativa L.) were grown in paddy soil treated with BCF and conventional fertilizer, respectively, for 30 days. The biochar-induced changes in nutrient accumulation in roots, and the elemental composition, distribution and speciation of the biomineral composites formed in the biochar-treated roots at the micron and sub-micron scale, were investigated by a range of techniques. Results of laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) showed that biochar treatment significantly increased concentrations of nutrients (e.g., Fe, Si, and P) inside the root. Raman mapping and vibrating sample magnetometry identified biochar particles and magnetic Fe nanoparticles associated with the roots. With Fe plaque formation, higher concentrations of FeOx− and FeOxH− anions on the root surface than the interior were detected by time-of-flight secondary ionization mass spectrometry (ToF-SIMS). Analysis of data from scanning electron microscopy energy-dispersive spectroscopy (SEM-EDS), and from scanning transmission electron microscopy (STEM) coupled with EDS or energy electron loss spectroscopy (EELS), determined that Fe(III) oxide nanoparticles were accumulated in the crystalline fraction of the plaque and were co-localized with Si and P on the root surface. Iron-rich nanoparticles (Fe–Si nanocomposites with mixed oxidation states of Fe and ferritin) in the root cortex were identified by using aberration-corrected STEM and in situ EELS analysis, confirming the biomineralization and storage of Fe in the rice root. The findings from this study highlight that the deposition of Fe-rich nanocomposites occurs with contrasting chemical speciation in the Fe plaque and cortex of the rice root. This provides an improved understanding of the element homeostasis in rice with biochar-mineral fertilization.

This study describes organic thin films prepared under a range of conditions from a model series of bis-N-alkyl chloro-triazines functionalized with short alkyl chains from ethyl to hexyl. The pure films were characterized using atomic force microscopy (AFM), X-ray diffraction (XRD), Raman spectroscopy, and X-ray photoelectron spectroscopy (XPS). When cast on mica, these compounds assemble as crystalline sheets made up of a synthetic bilayer along the crystallographic ab-plane with an internal hydrogen-bonded domain between external alkyl chains. These micron-scale surfaces stack along the c-axis, and increasing the alkyl chain length results in changes to the crystal morphology from needles to nanoscale plates. Thicker films produce nanoscale, pyramidal stacks of bilayers. Compared to atomically flat mica, a rougher, unetched silicon substrate produced irregular domains in the secondary bilayer. Films of mixtures comprising the ethyl derivative with butyl, pentyl, or hexyl derivative were imaged using time-of-flight secondary-ion mass spectrometry (ToF-SIMS) that indicated a trend toward a constant stoichiometry with increasing alkyl chain length. AFM of mixed films on mica showed single bilayers of height

In this study, we describe the synthesis and molecular properties of anthranilamide-based short peptides which were synthesised via ring opening of isatoic anhydride in excellent yields. These short peptides were incorporated as low molecular weight gelators (LMWG), bola amphiphile, and C3-symmetric molecules to form hydrogels in low concentrations (0.07–0.30% (w/v)). The critical gel concentration (CGC), viscoelastic properties, secondary structure, and fibre morphology of these short peptides were influenced by the aromaticity of the capping group or by the presence of electronegative substituent (namely fluoro) and hydrophobic substituent (such as methyl) in the short peptides. In addition, the hydrogels showed antibacterial activity against S. aureus 38 and moderate toxicity against HEK cells in vitro.

Recent studies have demonstrated the importance of the nutrient status of biochar and soils prior to its inclusion in particular agricultural systems. Pre-treatment of nutrient-reactive biochar, where nutrients are loaded into pores and onto surfaces, gives improved yield outcomes compared to untreated biochar. In this study we have used a wide selection of spectroscopic and microscopic techniques to investigate the mechanisms of nutrient retention in a high temperature wood biochar, which had negative effects on Chenopodium quinoa above ground biomass yield when applied to the system without prior nutrient loading, but positive effects when applied after composting. We have compared non-composted biochar (BC) with composted biochar (BCC) to elucidate the differences which may have led to these results. The results of our investigation provide evidence for a complex series of reactions during composting, where dissolved nutrients are first taken up into biochar pores along a concentration gradient and through capillary action, followed by surface sorption and retention processes which block biochar pores and result in deposition of a nutrient-rich organomineral (plaque) layer. The lack of such pretreatment in the BC samples would render it reactive towards nutrients in a soil-fertilizer system, making it a competitor for, rather than provider of, nutrients for plant growth.

In this study, we report the synthesis of glyoxylamide peptide-mimics as self-assembled gels with well-defined molecular structures for topical delivery of ciprofloxacin (CIP). The glyoxylamide peptide mimics successfully formed hydrogels with critical gel concentrations of 0.02-0.08% (w/v). The mechanical strength, secondary structure, and fiber morphology of these hydrogels can be modulated by varying the N-substituent of the ring-opened isatins. The synthesised hydrogel exhibited a high loading capacity of CIP (40% (w/w)) and a sustained release profile. The CIP-loaded hydrogels were able to release CIP for more than 15 days and the released solution was shown to retain activity against Gram-positive and Gram-negative bacteria. In addition, the hydrogels formed showed low toxicity against Cos7 cells.

This study describes a multivariate statistical model (derived using partial least squares regression, PLS-R) that derives charring intensity (reaction temperature and duration) from the attenuated total reflectance (ATR) Fourier Transform Infrared (FTIR) spectra of charcoal. Data for the model was obtained from a library of charcoal samples produced under laboratory conditions at charring intensities (CI) relevant to wildfires and a series of feedstocks representing common tree species collected from Australia. The PLS-R model developed reveals the potential of FTIR to determine the charring intensity of charcoal. Though limited by the differences between laboratory-produced charcoal and the more heterogeneous and less-structured charcoal produced in a wildfire, the method was tested against fossil charcoal from a well-dated sediment core collected from Thirlmere Lakes National Park, Australia and showed a distinct change in CI that can be related to other climatic and environmental proxies. We suggest that the method has the potential to offer insights into the conditions under which natural charcoal is formed including the modelling of charring intensities of fossil charcoal samples isolated from sediments, archaeological applications or characterisation of contemporary fire events from charcoal in soils.

Coagulation and flocculation (C-F) followed by a separation process such as sedimentation or dissolved air flotation is a major barrier to algal or cyanobacterial cells in water treatment plants and a common harvesting technique for algae cultured for high value products. Tailoring algal physical floc properties (size, strength, and density) has been shown to be important to optimise separation, however, the chemical properties of the flocs that lead to the physical properties are not yet well understood. This study investigated the biochemical composition of algal (Chlorella vulgaris) and cyanobacterial (Microcystis aeruginosa) flocs produced under sweep flocculation using aluminium sulphate as a coagulant. These flocs had very different physical properties. A new approach was developed to undertake biochemical characterisation of associated flocs using reflectance Fourier transform infrared (FTIR) imaging. Analysing the biochemical composition of the algal and cyanobacterial flocs revealed that the distribution of proteins and carbohydrates in the flocs are most likely responsible for the unique physical floc characteristics observed. The large flocs of C. vulgaris were characterised by a homogenous distribution of proteins and polysaccharides, and a high glycoprotein and biopolymer content. In contrast, the smaller but stronger flocs of M. aeruginosa had more concentrated protein regions within the flocs that tended to associate at the edge of regions which were absent of biomolecules, potentially comprising coagulant. Overall, the technique shows great potential for analysing algal flocs to gain a better understanding of the underlying biochemical composition and distribution of these biomolecules that leads to the varying physical floc properties.

The bis-N-alkyl-chlorotriazines show a strong tendency to form one-dimensional hydrogen-bonded tapes in the solid state. We predicted that increasing the alkyl chain length in the simplest tape-forming molecule would enable a controlled increase of the inter-tape spacing in the crystalline state. A series of bis-N-alkyl groups from bis-N-ethyl to bis-N-pentyl were synthesised and structurally characterised using single-crystal and powder X-ray diffraction at low temperature and ambient temperature. At low temperature the alkyl chains are rarely linear, instead adopting a variety of conformations to achieve close packing. Despite this variation, there is still a strong correlation of alkyl chain length with the inter-tape spacing in a single direction in the crystal. This correlation is strongest at ambient temperature where the longer chains are highly disordered and extended. We observe an “odd-number carbon” effect where bis-N-propyl 1b and bis-N-pentyl 1d derivatives undergo a structural phase transition with temperature.

The synthesis and supramolecular properties of novel glyoxylamide-based short peptides formed via the ring-opening reaction of N-acetylisatins in solution phase are described. The short peptides self-assembled into gels, which were examined for their mechanical and morphological characteristics using multiple spectroscopic and microscopy techniques. The critical gel concentration and mechanical strength of the self-assembled gels were influenced by the presence of electronegative substituents (such as fluoro, in 5b) or hydrophobic substituents (such as bromo, 5d) respectively in the short peptides. Moreover, in vitro cytotoxicity assays demonstrated that these compounds were non-toxic to mammalian cells.

Received April 28, 2015; revised June 5, 2015; accepted June 8, 2015. From the Department of Psychiatry, University of Vermont Medical Center, Burlington, VT (JCK, AMR, TR); Department of Surgery, Danbury Hospital, Danbury, CT (ASP); Department of Surgery, University of Vermont Medical Center, Burlington, VT (GTT); and Department of FamilyMedicine, University of VermontMedical Center, Burlington, VT (TR). Send correspondence and reprint requests to Julia C. Knight, M.D., Ph.D., Department of Psychiatry, University of Vermont Medical Center, 111 Colchester Ave, Burlington, VT 05401; e-mail: julia.knight@uvmhealth.org Published by Elsevier Inc. on behalf of The Academy of Psychosomatic Medicine. Introduction

The accumulation of redox-active transition metals in the brain and metal dyshomeostasis are thought to be associated with the etiology and pathogenesis of several neurodegenerative diseases, and Alzheimer’s disease (AD) in particular. As well, distinct biometal imaging and role of metal uptake transporters are central to understanding AD pathogenesis and aging but remain elusive, due inappropriate detection methods. We therefore hypothesized that Octodon degus develop neuropathological abnormalities in the distribution of redox active biometals, and this effect may be due to alterations in the expression of lysosomal protein, major Fe/Cu transporters, and selected Zn transporters (ZnTs and ZIPs). Herein, we report the distribution profile of biometals in the aged brain of the endemic Chilean rodent O. degus—a natural model to investigate the role of metals on the onset and progression of AD. Using laser ablation inductively coupled plasma mass spectrometry, our quantitative images of biometals (Fe, Ca, Zn, Cu, and Al) appear significantly elevated in the aged O. degus and show an age-dependent rise. The metals Fe, Ca, Zn, and Cu were specifically enriched in the cortex and hippocampus, which are the regions where amyloid plaques, tau phosphorylation and glial alterations are most commonly reported, whilst Al was enriched in the hippocampus alone. Using whole brain extracts, age-related deregulation of metal trafficking pathways was also observed in O. degus. More specifically, we observed impaired lysosomal function, demonstrated by increased cathepsin D protein expression. An age-related reduction in the expression of subunit B2 of V-ATPase, and significant increases in amyloid beta peptide 42 (Aβ42), and the metal transporter ATP13a2 were also observed. Although the protein expression levels of the zinc transporters, ZnT (1,3,4,6, and 7), and ZIP7,8 and ZIP14 increased in the brain of aged O. degus, ZnT10, decreased. Although no significant age-related change was observed for the major iron/copper regulator IRP2, we did find a significant increase in the expression of DMT1, a major transporter of divalent metal species, 5′-aminolevulinate synthase 2 (ALAS2), and the proto-oncogene, FOS. Collectively, our data indicate that transition metals may be enriched with age in the brains of O. degus, and metal dyshomeostasis in specific brain regions is age-related.

Direct analysis of the colonised surface on coal using attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) revealed the nature of bacteria-mediated oxidation at the coal surface. Unique oxidation peaks generated by the presence of Pseudomonas fluorescens on coal was shown through ATR-FTIR measurements, and ATR-FTIR imaging illustrated that this peak was only observed within the region of coal colonised by bacteria. Contact angle measurements and surface free energy of adhesion calculations showed that the adhesion between P. fluorescens and coal was thermodynamically favourable, and scanning electron microscopy (SEM) exhibited individual cell or monolayer cluster attachment on coal. Furthermore, Gaussian peak fitting of peroxidase-treated coal ATR-FTIR spectra revealed that peroxidase or related enzymes produced by P. fluorescens may be responsible for coal oxidation. This study demonstrated the usefulness and practicality of ATR-FTIR for analysing coal oxidation by P. fluorescens and may well be applied to other microbe-driven modifications of coal for its rapidity and reliability.

α-Hemoglobin (αHb)-stabilizing protein (AHSP) is a molecular chaperone that assists hemoglobin assembly. AHSP induces changes in αHb heme coordination, but how these changes are facilitated by interactions at the αHb·AHSP interface is not well understood. To address this question we have used NMR, x-ray absorption spectroscopy, and ligand binding measurements to probe αHb conformational changes induced by AHSP binding. NMR chemical shift analyses of free CO-αHb and CO-αHb·AHSP indicated that the seven helical elements of the native αHb structure are retained and that the heme Fe(II) remains coordinated to the proximal His-87 side chain. However, chemical shift differences revealed alterations of the F, G, and H helices and the heme pocket of CO-αHb bound to AHSP. Comparisons of iron-ligand geometry using extended x-ray absorption fine structure spectroscopy showed that AHSP binding induces a small 0.03 Å lengthening of the Fe-O2 bond, explaining previous reports that AHSP decreases αHb O2 affinity roughly 4-fold and promotes autooxidation due primarily to a 3-4-fold increase in the rate of O2 dissociation. Pro-30 mutations diminished NMR chemical shift changes in the proximal heme pocket, restored normal O2 dissociation rate and equilibrium constants, and reduced O2-αHb autooxidation rates. Thus, the contacts mediated by Pro-30 in wild-type AHSP promote αHb autooxidation by introducing strain into the proximal heme pocket. As a chaperone, AHSP facilitates rapid assembly of αHb into Hb when βHb is abundant but diverts αHb to a redox resistant holding state when βHb is limiting.

Recent interest in biochar characterisation has been driven by its effectiveness as a soil additive, where it can act as a carbon sink, a detoxification agent, and as a means to improve crop yields, especially when prepared as a char–mineral composite. Optimising biochar performance, raw material selection and manufacturing conditions, demands an understanding of structure and chemistry in these complex materials that typically comprise numerous minerals and organic phases. This study presents techniques to successfully image these challenging materials using Fourier transform infrared (FTIR) spectroscopy and Raman spectroscopy. The FTIR and Raman results are presented with results from scanning electron microscopy with energy dispersive X-ray spectroscopy (SEM–EDX), and X-ray photoelectron spectroscopy (XPS). We demonstrate that millimetre-scale organic phases are present in Acacia saligna biochar particles. Mineral enrichment of this biochar with bentonite-iron oxide generates new chemical phases, most likely through acid catalysed dehydration.

The thermodynamics of Zn(2+) binding to three peptides corresponding to naturally occurring Zn-binding sequences in transcription factors have been quantified with isothermal titration calorimetry (ITC). These peptides, the third zinc finger of Sp1 (Sp1-3), the second zinc finger of myelin transcription factor 1 (MyT1-2), and the second Zn-binding sequence of the DNA-binding domain of glucocorticoid receptor (GR-2), bind Zn(2+) with Cys(2)His(2), Cys(2)HisCys, and Cys(4) coordination, respectively. Circular dichroism confirms that Sp1-3 and MyT1-2 have considerable and negligible Zn-stabilized secondary structure, respectively, and indicate only a small amount for GR-2. The pK(a)'s of the Sp1-3 cysteines and histidines were determined by NMR and used to estimate the number of protons displaced by Zn(2+) at pH 7.4. ITC was also used to determine this number, and the two methods agree. Subtraction of buffer contributions to the calorimetric data reveals that all three peptides have a similar affinity for Zn(2+), which has equal enthalpy and entropy components for Sp1-3 but is more enthalpically disfavored and entropically favored with increasing Cys ligands. The resulting enthalpy-entropy compensation originates from the Zn-Cys coordination, as subtraction of the cysteine deprotonation enthalpy results in a similar Zn(2+)-binding enthalpy for all three peptides, and the binding entropy tracks with the number of displaced protons. Metal and protein components of the binding enthalpy and entropy have been estimated. While dominated by Zn(2+) coordination to the cysteines and histidines, other residues in the sequence affect the protein contributions that modulate the stability of these motifs.

Colorimetric (near-UV absorption spectroscopy) and calorimetric (isothermal titration calorimetry) methods have been used to quantify the equilibrium and thermodynamics of arsenite and monomethylarsenite (MMA) coordinating to glutathione (GSH) and the dithiols dimercaptosuccinic acid (DMSA), dihydrolipoic acid (DHLA), and dithiothreitol (DTT). We found that both arsenite and MMA form moderately stable complexes (beta = 10(6)-10(7)) with GSH; that arsenite forms a particularly stable 2:3 complex (beta approximately 10(18)) with the biological cofactor DHLA; that MMA has a somewhat higher affinity than arsenite for thiol ligands; and that entropic factors modulate the overall stability of As(III) complexes with thiols, which are favored by the exothermic formation of As(III)-thiolate bonds. The implications of these results for arsenic toxicity are discussed.

Hemoglobin A (HbA), the oxygen delivery system in humans, comprises two alpha and two beta subunits. Free alpha-hemoglobin (alphaHb) is unstable, and its precipitation contributes to the pathophysiology of beta thalassemia. In erythrocytes, the alpha-hemoglobin stabilizing protein (AHSP) binds alphaHb and inhibits its precipitation. The crystal structure of AHSP bound to Fe(II)-alphaHb reveals that AHSP specifically recognizes the G and H helices of alphaHb through a hydrophobic interface that largely recapitulates the alpha1-beta1 interface of hemoglobin. The AHSP-alphaHb interactions are extensive but suboptimal, explaining why beta-hemoglobin can competitively displace AHSP to form HbA. Remarkably, the Fe(II)-heme group in AHSP bound alphaHb is coordinated by the distal but not the proximal histidine. Importantly, binding to AHSP facilitates the conversion of oxy-alphaHb to a deoxygenated, oxidized [Fe(III)], nonreactive form in which all six coordinate positions are occupied. These observations reveal the molecular mechanisms by which AHSP stabilizes free alphaHb.

Alzheimer's disease (AD) is the leading cause of dementia in the elderly, affecting over 27 million people worldwide. AD represents a complex neurological disorder which is best understood as the consequence of a number of interconnected genetic and lifestyle variables, which culminate in multiple changes to brain structure and function. These can be observed on a gross anatomical level in brain atrophy, microscopically in extracellular amyloid plaque and neurofibrillary tangle formation, and at a functional level as alterations of metabolic activity. At a molecular level, metal dyshomeostasis is frequently observed in AD due to anomalous binding of metals such as Iron (Fe), Copper (Cu), and Zinc (Zn), or impaired regulation of redox-active metals which can induce the formation of cytotoxic reactive oxygen species and neuronal damage. Metal chelators have been administered therapeutically in transgenic mice models for AD and in clinical human AD studies, with positive outcomes. As a result, neuroimaging of metals in a variety of intact brain cells and tissues is emerging as an important tool for increasing our understanding of the role of metal dysregulation in AD. Several imaging techniques have been used to study the cerebral metallo-architecture in biological specimens to obtain spatially resolved data on chemical elements present in a sample. Hyperspectral techniques, such as particle-induced X-ray emission (PIXE), energy dispersive X-ray spectroscopy (EDS), X-ray fluorescence microscopy (XFM), synchrotron X-ray fluorescence (SXRF), secondary ion mass spectrometry (SIMS), and laser ablation inductively coupled mass spectrometry (LA-ICPMS) can reveal relative intensities and even semi-quantitative concentrations of a large set of elements with differing spatial resolution and detection sensitivities. Other mass spectrometric and spectroscopy imaging techniques such as laser ablation electrospray ionization mass spectrometry (LA ESI-MS), MALDI imaging mass spectrometry (MALDI-IMS), and Fourier transform infrared spectroscopy (FTIR) can be used to correlate changes in elemental distribution with the underlying pathology in AD brain specimens. Taken together, these techniques provide new techniques to probe the pathobiology of AD and pave the way for identifying new therapeutic targets. The current review aims to discuss the advantages and challenges of using these emerging elemental and molecular imaging techniques, and highlight clinical achievements in AD research using bioimaging techniques.

Cytochrome c (cyt c) is a small heme protein (MW 12 384) that functions as a biological electron-transfer agent. It consists of a single polypeptide chain and a prosthetic heme group and provides a pathway for the transfer of electrons from cyt c reductase to cyt c oxidase in the mitochondrial respiratory chain (oxidative phosphorylation). The protein participates in oxidation-reduction reactions with the heme iron alternating between the oxidized (ferric, Fe{sup III}) state and the reduced (ferrous, Fe{sup II}) state. X-ray absorption fine structure (XAFS) data were obtained from frozen aqueous solutions (10 K) of horse heart ferri- and ferrocyt c. Models of the structure about the Fe center were refined to optimize the fit between the observed XAFS in the range 0 {le} k {le} 16.3 {angstrom}{sup {minus}1} and the XAFS calculated using both single-scattering (SS) and multiple-scattering (MS) calculations. The bond lengths obtained are more accurate and precise than those determined previously for cyt c from various species using X-ray crystallography. The Fe-N bond lengths are 1.98--1.99 {angstrom} for both oxidation states of cyt c. The Fe-S bond of derricyt c (2.33 {angstrom}) is significantly longer than that of ferrocyt c (2.29 {angstrom}). The small changes in themore » bond lengths are consistent with the small reorganizational energy required for the fast electron-transfer reaction of cyt c.« less

XAFS data in the range 0 ≤ k ≤ 14.5 A-1 have been obtained from frozen aqueous solutions (10 K) of horse heart myoglobin (Mb) in the Fe(III) (aqua-met) and Fe(II) (deoxy) forms. The structures of the Fe sites have been refined using both single-scattering (SS) and multiple-scattering (MS) analyses. The XAFS MS analyses yield more precise Fe−ligand bond lengths (estimated error 0.02−0.03 A) than those determined crystallographically (estimated errors ≥0.1 A). For met-Mb, the MS analysis results in an average Fe−N(pyrrole) distance of 2.05 A, an Fe−N(imidazole) distance of 2.17 A, and an Fe−O(aqua) distance of 2.08 A. For deoxy-Mb, the MS analysis results in Fe−N(pyrrole) and Fe−N(imidazole) distances of 2.06 and 2.16 A, respectively. The final XAFS R values are 18.8% and 17.8% for met- and deoxy-Mb, respectively. The robustness of the refinements was tested by varying the starting models, constraints, restraints, and k ranges.

The structural characterizations of the Fe environments in the NO adducts of horse heart ferric (FeIII) and ferrous (FeII) nitrosylmyoglobin (MbNO) have been achieved by multiple-scattering (MS) an...

Duloxetine hydrochloride (1) is an important antidepressant that acts as a serotonin and noradrenaline reuptake inhibitor that has only recently been characterized by single-crystal X-ray diffraction. This study describes an investigation into polymorphism of duloxetine hydrochloride, discusses the challenges of characterizing new structures, and reports a new metastable solvate (1(acetone)) where acetone is trapped in a duloxetine hydrochloride host lattice. In view of the importance of formulation processing and bioavailability characteristics of the crystalline forms of 1, a comprehensive structural study of 1(acetone) was carried out using single-crystal and powder X-ray diffraction, infrared and Raman spectroscopies, and solid-state NMR spectroscopy. The rapid desolvation from 1(acetone) to the stable unsolvated form was investigated, and the structures of free and solvated forms are discussed in terms of the noncovalent intermolecular interactions.

Copper K-edge X-ray absorption spectroscopic (XAS) measurements were recorded for the veterinary antiinflammatory Cu(II) complexes of indomethacin (1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indole-3-acetic acid = IndoH), of the general formula [Cu(2)(Indo)(4)L(2)] (L = N,N-dimethylformamide (DMF), N,N-dimethylacetamide (DMA), N-methylpyrrolidone (NMP), and water), and [Cu(2)(OAc)(4)(OH(2))(2)] at room temperature and 10 K. The bond lengths and bridging O-C-O angles of the dimeric Cu(II) cage (Cu(2)O(10)C(8)) obtained from the multiple-scattering (MS) fitting of the X-ray absorption fine structure (XAFS) using a centrosymmetric model of [Cu(2)(Indo)(4)(DMF)(2)] gave Cu.Cu = 2.62(2) A, mean Cu-O(Ac) = 1.95(2) A, Cu-O(L) = 2.15(2) A, bridging O-C-O = 125(1) degrees, Cu displacement from plane 0.19 A compared with the XRD data Cu.Cu = 2.630(1) A, mean Cu-O(Ac) = 1.959 A, Cu-O(L) = 2.143(5) A, bridging O-C-O angles = 123.2(5) degrees, Cu displacement from plane 0.20 A. The excellent agreement between the XAFS- and XRD-derived data allowed the structures of related [Cu(2)(Indo)(4)L(2)] (L = DMA, NMP) complexes to be determined. All display a similar Cu(2)O(10)C(8) coordination geometry, which is independent of the nature of the axial ligand. While XAFS analysis of [Cu(2)(Indo)(4)(OH(2))(2)] and [Cu(2)(OAc)(4)(OH(2))(2)] indicates a coordination geometry similar to that of [Cu(2)(Indo)(4)L(2)] (L = DMF, DMA, NMP), removal of symmetry restraints in the MS model is required to obtain axial bond lengths comparable to those derived in the XRD structures of the acetate complex. For the Indo complex, the fitted bond lengths with the lower symmetry model give a mean Cu-L(OH2) bond distance within experimental errors of the value for [Cu(2)(Indo)(4)(DMSO)(2)] (2.16(2) A) (XRD). The difficulty in refining the Cu-O(OH2) distance of [Cu(2)(OAc)(4)(OH(2))(2)] and [Cu(2)(Indo)(4)(OH(2))(2)] using a centrosymmetric MS model is attributed to a symmetry reduction due to hydrogen-bonding effects characteristic of the aqua adducts, as is observed in the XRD structure of the acetate complex.

This mini-review outlines the current theories on the mechanism of electron transfer from water to P680, the location and structure of the water oxidising complex and the role of the manganese cluster. We discuss how our data fit in with current theories and put forward our ideas on the location and mechanism of water oxidation.

The NO adducts of leghemoglobin (Lb) are implicated in biological processes, but only the adduct with ferrous Lb (Lb(II)NO) has been characterized previously. We report the first characterization of ferric nitrosylleghemoglobin (Lb(III)NO) and XAS experiments performed on frozen aqueous solutions of Lb(II)NO and Lb(III)NO at 10 K. The XANES and electronic spectra of the NO adducts are similar in shape and energies to the myoglobin (Mb) analogues. The environment of the Fe atom has been refined using multiple-scattering (MS) analyses of the XAFS data. For Lb(II)NO, the MS analysis resulted in an averaged Fe-N(p)(pyrrole) distance of 2.02 A, an Fe-N(epsilon)(imidazole) distance of 1.98 A, an Fe-N(NO) distance of 1.77 A, and an Fe-N-O angle of 147 degrees. The Fe-N(NO) distance and Fe-N-O angle obtained from the analysis of Lb(II)NO are in good agreement with those determined crystallographically for [Fe(TPP)(NO)] (TPP, tetraphenylporphyrinato), with and without 1-methylimidazole (1-MeIm) as the sixth ligand, and the MS XAFS structures reported previously for the myoglobin (Mb(II)NO) analogue and [Fe(TPP)(NO)]. The MS analysis of Lb(III)NO yielded an average Fe-N(p) distance of 2.00 A, an Fe-N(epsilon) distance of 1.89 A, an Fe-N(NO) distance of 1.68 A, and an Fe-N-O angle of 173 degrees. These bond lengths and angles are consistent with those determined previously for the myoglobin analogue (Mb(III)NO) and the crystal structures of the model complexes, [Fe(III)(TPP)(NO)(OH(2))](+) and [Fe(OEP)(NO)](+) (OEP, octaethylporphyrinato). The final XAFS R values were 16.1 and 18.2% for Lb(II)NO and Lb(III)NO, respectively.

The title compound [systematic name: N-methyl-3-(1-naphthyloxy)-3-(2-thienyl)propan-1-aminium chloride], C18H20NOS+·Cl−, was crystallized from 1,4-dioxane. Twofold rotational disorder exhibited by the thiophene ring in a 0.580 (5):0.420 (5) ratio represents two different conformations of the molecule that exist in the same crystal form. The crystal structure contains strong N—H...Cl hydrogen bonds.

The interaction of water oxidising photosystem II preparations with the aqueous environment has been investigated using electron spin echo envelope modulation spectroscopy in the presence of 2H(2)O. The spectra show interaction of 2H of 2H(2)O with the preparation in the S(2) state. The component interacting with water decays during 1-4 weeks storage at 77 K. No interaction of water with the classical multiline S(2) Mn signal, which is more stable on storage at 77 K, was detected. The results show that a component of the water oxidation complex, possibly involving the Mn centre, is accessible to water and may be the water binding site for photosynthetic water oxidation.