14090-81-4

Upstream product

• 766-92-7 [(methylthio)methyl]-benzene 
• 824-86-2 benzylmethylsulfoxide 
• 16601-40-4 S-benzyl phenyl-methanethiosulfonate 
• 75-16-1 methylmagnesium bromide 
• 827307-99-3 (4S,5R,S_S)-cis-N-(benzylsulfinyl)hexahydrobenzoxazolidin-2-one 
• 63520-69-4 (-)-cholesteryl (-)-(S)-methanesulfinate 
• 135802-77-6 (S_S)-1,2:5,6-di-O-isopropylidene-α-D-glucofuranosyl methanesulfinate 
• 827307-95-9 cis-(4S,5R)-N-(benzylthio)hexahydrobenzoxazolidinone 
• 827307-94-8 trans-(4R,5R)-N-(benzylthio)hexahydrobenzoxazolidinone 

Downstream Products

• 29293-45-6 C₈H₉⁽²⁾HOS 
• 344295-54-1 <α-2H>benzyl methyl sulfone 

Relevant academic research and scientific papers

Asymmetric Sulfoxidation using oxaziridine

oxaziridine oxidizes sulfides to sulfoxides cleanly and efficiently in up to 98percent ee.

A click chemistry approach towards flavin-cyclodextrin conjugates-bioinspired sulfoxidation catalysts

A click chemistry approach based on the reaction between alkynylflavins and mono(6-azido-6-deoxy)-β-cyclodextrin has proven to be a useful tool for the synthesis of flavin-cyclodextrin conjugates studied as monooxygenase mimics in enantioselective sulfoxi

The mutagenesis of a single site for enhancing or reversing the enantio- or regiopreference of cyclohexanone monooxygenases

The mutagenesis of a "second sphere"switch residue of CHMOAcineto could control its enantio- and regiopreference. Replacing phenylalanine (F) at position 277 of CHMOAcineto into larger tryptophan (W) enabled a significant enhancement of enantio- or regioselectivity toward structurally diverse substrates, moreover, a complete reversal of enantio- or regiopreference was realized by mutating F277 into a range of smaller amino acids (A/C/D/E/G/H/I/K/L/M/N/P/Q/R/S/T/V).

Highly Efficient Access to (S)-Sulfoxides Utilizing a Promiscuous Flavoprotein Monooxygenase in a Whole-Cell Biocatalyst Format

Chiral sulfoxides have gained attention as synthons and precursors for API synthesis. Flavoproteins such as Baeyer-Villiger or styrene monooxygenases mainly provide access to (R)-sulfoxides and often suffer from low selectivity, activity, and/or limited substrate scope. The flavoprotein monooxygenase AbIMO from Acinetobacter baylyi ADP1 initiates indole degradation. Here, AbIMO was expressed recombinantly in E. coli and characterized for its sulfoxidation activity and substrate spectrum. Next to indole and styrene, AbIMO was found to accept numerous alkyl aryl sulfides as substrates, transforming them to (S)-sulfoxides with high enantioselectivity (95 percent to '99 percent for most sulfides). The formulation as a whole-cell biocatalyst allowed specific production rates of up to 370 U gcdw?1 – the highest specific oxygenase activity achieved in whole cells so far – and the preparative synthesis of enantiopure (S)-aryl alkyl sulfoxides. With its extraordinarily high specific activity, high specificity, ease of handling, and high stability (catalyst is stable for '16 days at 4 °C), the designed whole-cell biocatalyst adds enormous value to the portfolio of chemical and biological catalysts for asymmetric sulfoxide synthesis.

Accessing Enantiopure Epoxides and Sulfoxides: Related Flavin-Dependent Monooxygenases Provide Reversed Enantioselectivity

Enantiopure organic compounds are of major importance for the chemical and pharmaceutical industry. Flavin-dependent group E monooxygenases, composed of monooxygenase and reductase, are known to perform epoxidation of substituted alkenes as well as sulfoxidation in a regio- and enantioselective fashion. Group E is divided into styrene monooxygenases (SMO) and indole monooxygenases (IMO). Hitherto mainly SMOs have been characterized. In this study, we assayed 31 monooxygenases from both types, while 23 of which showed activity. They almost exclusively produced (S)-styrene oxide at high enantiomeric excess with maximum activities of 0.73 μmol min?1 mg?1 (kcat=0.54 s?1). In case of sulfoxidation, we found that the enantioselectivity is contrary between both types. IMOs preferably produce the (S)-enantiomer while SMOs have a tendency to produce the (R)-enantiomer. Sequence analysis and molecular docking of substrates allowed identifying fingerprint motives: SMO N46-V48-H50-Y73-H76-S96 and IMO S46-Q48-M50-V/I73-I76-A96. These form an essential part of the active site while the loop (AS44-51) interacts with the co-substrate and other amino acids direct the substrate. The motives clearly distinguish group E monooxygenases and define the enantioselectivity and thus direct biotechnological applications. Two-hour biotransformations with several sulfides in conjunction with upscale experiments (10 and 100 mg scale) resulted in the identification of promising candidates for the realization of biocatalytic processes.

Enzymatic kinetic resolution of chiral sulfoxides-an enantiocomplementary approach

A new enzymatic assay for the preparation of chiral sulfoxides that is enantiocomplementary to the known (S)-enantiomer-reducing activity of methionine sulfoxide reductase A (MsrA) is described. To this end, we have utilized the enzyme DMSO reductase (DmsABC), recently discovered by us being highly upregulated in stationary phase E. coli bacteria.

Stereoselective sulfoxidation catalyzed by achiral Schiff base complexes in the presence of serum albumin in aqueous media

Four coordination complexes ML derived from an achiral Schiff base ligand (H2L = 2,2′-[(1,2-ethanediyl)bis(nitrilopropylidyne)]bisphenol) have been synthesized and characterized. A method is described for the enantioselective oxidation of a series of aryl alkyl sulfides using the coordination complexes in the presence of serum albumins (SAs) in an aqueous medium at ambient temperature. The mixture of metal complexes with serum albumins is useful for inducing asymmetric catalysis. The complex, albumin source and substrate influence stereoselective sulfoxidation. At optimal pH with the appropriate oxidant, some of ML/SA systems are identified as very efficient catalysts, giving the corresponding sulfoxides in excellent chemical yield (up to 100%) and good enantioselectivity (up to 94% ee) in certain cases. UV–visible spectroscopic data provide evidence that stronger binding between the complex and serum albumin lead to higher enantioselectivity.

HPLC enantioseparation on a homochiral MOF-silica composite as a novel chiral stationary phase

The last frontier in the development of chiral stationary phases for chromatographic enantioseparation involves homochiral metal-organic frameworks (MOFs). Using enantiopure (R)-2,2′-dihydroxy-1,1′-binaphthalene-6,6′-dicarboxylic acid as a starting material, we prepared three homochiral MOFs that were further used as chiral stationary phases for high-performance liquid chromatography to separate the enantiomers of various kinds of racemic sulfoxides, sec-alcohols, β-lactams, benzoins, flavanones and epoxides. The experimental results showed excellent performances for enantioseparation, and highlighted that enantioseparation on homochiral MOF columns is practical.

Biotransformation of prochiral sulfides into (R)-sulfoxides using immobilized Gordonia terrae IEGM 136 cells

Biotransformation of methyl phenyl sulfide (MPS) into optically active (R)-sulfoxide was optimized using Gordonia terrae IEGM 136 cells immobilized into cryogel of polyvinyl alcohol. Biotransformation time of 0.5 g/L MPS was shortened from 144 to 24 h in comparison with free cells. Immobilized Gordonia cells were resistant to high (up to 1.5 g/L) sulfide concentrations and catalyzed its complete bioconversion into (R)-sulfoxide (95% ee) within 72 h. Using a sequential addition method, the total load of MPS reached 4.25 g/L. At that, MPS bioconversion was 96.9% and the enantiomeric excess (ee) value of the target (R)-sulfoxide was as high as 96%. Possible reuse of immobilized cells for MPS biotransformation was experimentally proved. The obtained biocatalyst showed a high activity towards ethyl phenyl sulfide, benzyl methyl sulfide, methyl p-tolyl sulfide and formed corresponding (R)-sulfoxides with 77-95% ee. Putative pathways for sulfide oxidation by Gordonia cells were proposed.

Asymmetric catalytic sulfoxidation by a novel v IV 8 cluster catalyst in the presence of serum albumin: A simple and green oxidation system

A novel VIV8 cluster formulated as [V8O12(OH)4(CH3O)4(DAC)4]·7CH3OH (1) (DAC = 1,2-diaminocyclohexane) has been constructed successfully. Enantioselective oxidation of a series of alkyl aryl sulfides catalyzed by 1 is tested in an aqueous medium in the presence of serum albumin. The catalytic procedure is found to be simple and environmentally friendly. The influences of the parameters such as concentration of catalyst and oxidant, pH, and reaction time on the thioanisole as models are investigated. Under optimum conditions, 1 exhibits high conversion (up to 99%), excellent chemoselectivity (≥90% in all cases) and moderate enantioselectivity (up to 75% ee). After binding with serum albumin, the catalytic activity of 1 is promoted. The bovine serum albumin (BSA) and pig serum albumin (PSA) molecules have a more positive effect on the catalytic activity.