2386-57-4Relevant articles and documents
Catalytic activity and anion activation in SN2 reactions promoted by complexes of silicon polypodands. Comparison with traditional polyethers
Maia, Angelamaria,Landini, Dario,Betti, Cecilia,Leska, Boguslawa,Schroeder, Grzegorz
, p. 1195 - 1198 (2005)
The catalytic activity of silicon polypodands was evaluated in anion-promoted reactions under solid-liquid phase-transfer catalysis (SL-PTC) conditions and compared with that exhibited by common PTC agents. Results showed that these many-armed ligands are
Predicting the hydrolytic breakdown rates of organophosphorus chemical warfare agent simulants using association constants derived from hydrogen bonded complex formation events
Chu, Dominique F.,Clark, Ewan R.,Ellaby, Rebecca J.,Hiscock, Jennifer,Pépés, Antigoni
, (2021/11/22)
Organophosphorus (OP) chemical warfare agents (CWAs) represent an ongoing global threat, through either purposeful environmental release or the need to dispose of historic stockpiles. This presents a need for the development of novel decontamination technologies. Due to the toxic nature and legal limitations placed on OP CWAs, the use of appropriate OP simulants that mimic the reactivity but not the toxicity of the agents themselves is vital to decontamination studies. Herein, we show that association constants derived from non-specific hydrogen bonded complexation events may be used as parameters within models to predict simulant reactivity. We also discuss the limitations that should be placed on such data.
Methanesulfonyl Iodide
Rajakaruna, Pradeepa,Gorden, John D.,Stanbury, David M.
supporting information, p. 14752 - 14759 (2019/11/11)
Methanesulfonyl iodide is produced in aqueous solutions from the reaction of triiodide with methanesulfinate. Dichroic crystals of (CH3SO2I)4·KI3·2I2 are formed from KI/I2 solutions with high concentrations of CH3SO2-, while dichroic crystals of (CH3SO2I)2·RbI3 are formed from RbI/I2 solutions. X-ray crystallography of these two compounds shows that the CH3SO2I molecules coordinate through their oxygen atoms to the metal cations and that the S-I bond length is 2.44 ?. At low concentrations of CH3SO2-, the solutions remain homogeneous and the sulfonyl iodide is formed in a rapid equilibrium: CH3SO2- + I3- ? CH3SO2I + 2I-, KMSI = 1.07 ± 0.01 M at 25 °C (μ = 0.1 M, NaClO4). The sulfonyl iodide solutions display an absorbance maximum at 309 nm with a molar absorptivity of 667 M-1 cm-1. Stopped-flow studies reveal that the equilibrium is established within the dead time of the instrument (～2 ms). Solutions of CH3SO2I decompose slowly to form the sulfonate: CH3SO2I + H2O → CH3SO3- + I- + 2H+, khyd. In dilute phosphate buffer, this decomposition occurs with khyd = 2.0 × 10-4 s-1 the decomposition rate shows an inverse-squared dependence on [I-] because of the KMSI equilibrium.
The reduced flavin-dependent monooxygenase SfnG converts dimethylsulfone to methanesulfinate
Wicht, Denyce K.
, p. 159 - 166 (2016/07/22)
The biochemical pathway through which sulfur may be assimilated from dimethylsulfide (DMS) is proposed to proceed via oxidation of DMS to dimethylsulfoxide (DMSO) and subsequent conversion of DMSO to dimethylsulfone (DMSO2). Analogous chemical oxidation processes involving biogenic DMS in the atmosphere result in the deposition of DMSO2 into the terrestrial environment. Elucidating the enzymatic pathways that involve DMSO2 contribute to our understanding of the global sulfur cycle. Dimethylsulfone monooxygenase SfnG and flavin mononucleotide (FMN) reductase MsuE from the genome of the aerobic soil bacterium Pseudomonas fluorescens Pf0-1 were produced in Escherichia coli, purified, and biochemically characterized. The enzyme MsuE functions as a reduced nicotinamide adenine dinucleotide (NADH)-dependent FMN reductase with apparent steady state kinetic parameters of Km = 69 μM and kcat/Km = 9 min?1 μM ?1 using NADH as the variable substrate, and Km = 8 μM and kcat/Km = 105 min?1 μM ?1 using FMN as the variable substrate. The enzyme SfnG functions as a flavoprotein monooxygenase and converts DMSO2 to methanesulfinate in the presence of FMN, NADH, and MsuE, as evidenced by 1H and 13C nuclear magnetic resonance (NMR) spectroscopy. The results suggest that methanesulfinate is a biochemical intermediate in sulfur assimilation.
