7783-06-4Relevant articles and documents
Factors affecting the hydrogen reduction kinetics of CsHSO4
Ponomareva,Lavrova
, p. 85 - 89 (2009)
The hydrogen reduction of CsHSO4, including in the presence of catalysts, is studied. The main factors affecting the rate of the process are determined. A possible reaction mechanism through the surface hydrated phase is discussed. Experiments
Fresenius, R.
, p. 339 - 339 (1887)
Tsang
, p. 1498 (1964)
Thompson, C. J. T.,Meyer, R. A.,Ball, J. S.
, p. 3284 - 3287 (1952)
Reaction between sulfur hexafluoride and hydrogen iodide
Padma,Vasudeva Murthy
, p. 1653 - 1654 (1964)
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Malisoff,Marks
, p. 1114,1118, 1119 (1931)
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McCoy,Weiss
, p. 1928,1930 (1954)
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Vogel, E.
, p. 214 (1875)
Meites, L.
, p. 4479 - 4481 (1951)
Bacon, R. F.,Fanelli, R.
, p. 639 - 648 (1943)
Wallenfels, K.,Hofmann, D.
, (1962)
Roth, H.
, p. 379 - 392 (1951)
Bock et al.
, p. 1663 (1977)
Samahy et al.
, p. 3177 (1964)
Vasudeva Murthy, A. R.
, p. 23 - 28 (1953)
LATTICE VIBRATION SPECTRA Part LXIV. Raman spectroscopic study of lithium hydrogensulfide LiSH: dynamic disorder and order-disorder phase transition
Beckenkamp, K.,Lutz, H. D.,Jacobs, H.,Metzner, U.
, p. 203 - 213 (1991)
Raman spectra (4000-50 cm-1) of lithium hydrogensulfide are recorded in the range from 70 to 300 K.The temperature dependence of frequencies and halfwidths of the SH- stretching and librational modes yields clear evidence for a disorder-order phase transition at 222 K and thermally activated dynamic disorder of the SH- ions in the room temperature polymorph.Down to 70 K the increasing splitting of the in-plane libration can be interpreted by a Landau-type order parameter.This splitting reflects increasing dynamic interactions (factor group splitting) of adjacent (in ) SH- ions due to the ordering process.The halfwidths of the stretching and out-of-plane librational modes exhibits an Arrhenius-type behaviour.The activation energies derived are 1.9 kJ mol-1 for both vibrations.The activation temperature (230 K) is in good agreement with that of the change of the specific heat at 228 K.The order mechanism and a plausible structure of the ordered phase below 222 K are discussed.
Kroto,Suffolk
, p. 545 (1972)
George, Z. M.
, p. 218 - 224 (1974)
Reynolds, E. J.
, p. 146 - 147 (1864)
Synthesis and X-ray diffraction characterization of FeNdSbS4, an analog of berthierite
Gasymov,Gasymova,Aliev
, p. 1095 - 1096 (2004)
A rare-earth-containing analog of the mineral berthierite, with the composition FeNdSbS4, was synthesized for the first time. FeNdSbS4 is isostructural with FeSb2S4 and crystallizes in orthorhombic symmetry (sp. gr. Pbam, Z = 4) with lattice parameters a = 11.395 A, b = 14.136 A, and c = 3.747 A.
Packer,Winchester
, p. 826 (1968)
Wendt,Landauer
, p. 510 (1922)
Dubois,M.R.,Vanderveer,M.C.,Dubois,D.L.
, p. 7456 (1980)
Edwards, J. G.,Wiedemeier, H.,Gilles, P. W.
, p. 2935 - 2938 (1966)
Sulfur-33 Isotope Tracing of the Hydrodesulfurization Process: Insights into the Reaction Mechanism, Catalyst Characterization and Improvement
Sushkevich, Vitaly L.,Popov, Andrey G.,Ivanova, Irina I.
, p. 10872 - 10876 (2017)
The novel approach based on 33S isotope tracing is proposed for the elucidation of hydrodesulfurization (HDS) mechanisms and characterization of molybdenum sulfide catalysts. The technique involves sulfidation of the catalyst with 33S-isotope-labeled dihydrogen sulfide, followed by monitoring the fate of the 33S isotope in the course of the hydrodesulfurization reaction by online mass spectrometry and characterization of the catalyst after the reaction by temperature-programmed oxidation with mass spectrometry (TPO-MS). The results point to different pathways of thiophene transformation over Co or Ni-promoted and unpromoted molybdenum sulfide catalysts, provide information on the role of promoter and give a key for the design of new efficient HDS catalysts.
Polymersome Wound Dressing Spray Capable of Bacterial Inhibition and H2S Generation for Complete Diabetic Wound Healing
Liu, Danqing,Liao, Yuyao,Cornel, Erik Jan,Lv, Mingchen,Wu, Tong,Zhang, Xinyue,Fan, Liujie,Sun, Min,Zhu, Yunqing,Fan, Zhen,Du, Jianzhong
, p. 7972 - 7985 (2021/11/01)
Diabetic wounds are difficult to heal due to recurrent bacterial infection, decreased proliferation, and migration of epidermal and endothelial cells. This is related to impaired leukocyte function and low blood concentrations of H2S in diabetic patients. Herein, an antibacterial polymersome-based wound dressing spray was demonstrated for complete diabetic wound healing. The designed polymersome was self-assembled from poly(?-caprolactone)24-block-poly[lysine15-stat-(S-aroylthiooxime)23] [PCL24-b-P(Lys23-stat-SATO15)], where PCL is the hydrophobic membrane-forming block and P(Lys-stat-SATO) acts as a hydrophilic stabilizer block. The polymersomes can penetrate and kill Gram-positive and Gram-negative bacteria because of the electrostatic interaction induced by the antibacterial P(Lys23-stat-SATO15) block. Furthermore, the SATO segments are capable of long-term H2S generation by reacting with cysteine (up to 12 h). This promotes proliferation, migration of epidermal and endothelial cells, and angiogenesis. Overall, this polymersome-based wound dressing spray acts as a bacterial inhibitor and H2S generator and offers a fresh insight into the effective treatment of diabetic wounds.
Evolution of Structural, Thermal, Optical, and Vibrational Properties of Sc2S3, ScCuS2, and BaScCuS3 Semiconductors
Aleksandrovsky, Aleksandr S.,Andreev, Oleg V.,Azarapin, Nikita O.,Leonidov, Ivan I.,Maximov, Nikolai G.,Oreshonkov, Aleksandr S.,Razumkova, Illaria A.,Shestakov, Nikolai P.
, p. 3355 - 3366 (2021/08/23)
In the present work, we report on the synthesis of Sc2S3, ScCuS2 and BaScCuS3 powders using a method based on oxides sulfidation and modification of their properties. The crystal structures and morphology of samples are verified by XRD and SEM techniques. Thermal stability has been studied by DTA which has revealed that Sc2S3 decomposes to ScS through melting at 1877 K. ScCuS2 and BaScCuS3 melt incongruently at temperatures of 1618 K and 1535 K, respectively. The electronic structure calculations show that the investigated compounds are semiconductors with indirect band gap (Eg). According to the diffuse reflection spectroscopy, Sc2S3, ScCuS2 and BaScCuS3 are wide-bandgap semiconductors featured the Eg values of 2.53 eV, 2.05 eV and 2.06 eV, respectively. The band gap decreases with the introduction of copper (I) and barium cations into the crystal structure of the compounds. Variation of local structure has been verified by Raman and infrared spectroscopy. The calculated vibrational modes of ScCuS2 correspond to CuS4 and Sc?S layer vibrations, even though ScS6 octahedra-like structural units can be found in the structure.
In Vitro Reconstitution of a Five-Step Pathway for Bacterial Ergothioneine Catabolism
Beliaeva, Mariia A.,Leisinger, Florian,Seebeck, Florian P.
, p. 397 - 403 (2021/03/08)
Ergothioneine is a histidine-derived sulfur metabolite that is biosynthesized by bacteria and fungi. Plants and animals absorb ergothioneine as a micronutrient from their environment or nutrition. Several different mechanisms of microbial ergothioneine production have been described in the past ten years. Much less is known about the genetic and structural basis for ergothioneine catabolism. In this report, we describe the in vitro reconstitution of a five-step pathway that degrades ergothioneine to l-glutamate, trimethylamine, hydrogen sulfide, carbon dioxide, and ammonia. The first two steps are catalyzed by the two enzymes ergothionase and thiourocanate hydratase. These enzymes are closely related to the first two enzymes in histidine catabolism. However, the crystal structure of thiourocanate hydratase from the firmicute Paenibacillus sp. reveals specific structural features that strictly differentiate the activity of this enzyme from that of urocanate hydratases. The final two steps are catalyzed by metal-dependent hydrolases that share most homology with the last two enzymes in uracil catabolism. The early and late part of this pathway are connected by an entirely new enzyme type that catalyzes desulfurization of a thiohydantoin intermediate. Homologous enzymes are encoded in many soil-dwelling firmicutes and proteobacteria, suggesting that bacterial activity may have a significant impact on the environmental availability of ergothioneine.