18453-46-8

Basic information

• Product Name: Benzene, [(S)-methylsulfinyl]-
• CAS NO: 18453-46-8
• Molecular Formula: C7H8OS
• Molecular Weight: 140.206
• Mol File: 18453-46-8.mol

Chemical Properties

• CAS DataBase Reference: Benzene, [(S)-methylsulfinyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzene, [(S)-methylsulfinyl]-(18453-46-8)
• EPA Substance Registry System: Benzene, [(S)-methylsulfinyl]-(18453-46-8)

Safety Data

• Hazardous Substances Data: 18453-46-8(Hazardous Substances Data)

Upstream product

• 100-68-5 methyl-phenyl-thioether 
• 1193-82-4 racemic methyl phenyl sulfoxide 
• 227952-63-8 (S)-diethyl (phenylsulfinyl)methylphosphonate 
• 5535-48-8 PVS 
• 29290-71-9 2-(phenylsulfanyl)ethyl phenyl sulfone 
• 58921-74-7 2-(phenylsulfinyl)ethyl phenyl sulfone 
• 74-88-4 methyl iodide 
• 14173-25-2 methyl phenyl disulfide 
• 4032-81-9 ethyl phenyl disulfide 
• 135802-77-6 (S_S)-1,2:5,6-di-O-isopropylidene-α-D-glucofuranosyl methanesulfinate 
• 114026-76-5 (-)-(2R,3R)-trans-2,3-bis(hydroxydiphenylmethyl)-1,4-dioxaspiro[4.5]decane 
• 42843-29-8 Methanesulfinic acid (R)-((1S,2R)-2-hydroxy-1-methyl-2-phenyl-ethyl)-methyl-amide 
• 917-54-4 methyllithium 
• 77382-90-2 (S)-o-<1-((S)-1-α-naphtylethylamino)ethyl>phenol 

Downstream Products

• 4381-25-3 (S)-S-methyl-S-phenylsulfoximine 
• 560087-80-1 (S)-ethyl 2-(phenylsulfinyl)acetate 
• 60933-65-5 (R)-S-methyl-S-phenylsulfoximine 
• 1316846-41-9 C₂₉H₄₆O₈SSi 
• 1316846-40-8 C₂₅H₃₈O₆SSi 
• 1316846-39-5 C₂₅H₃₆O₅SSi 
• 1316846-38-4 C₁₉H₂₂O₅S 
• 1316846-35-1 C₁₉H₂₃BrO₅S 
• 1316846-50-0 C₂₈H₄₂O₆SSi 
• 1316846-49-7 C₂₂H₂₉NO₁₀S 
• 1316846-48-6 C₂₄H₄₃NO₈SSi 
• 1316846-47-5 C₂₅H₄₃NO₇SSi 
• 1316846-45-3 C₂₇H₄₉NO₇S₂Si 

Relevant articles and documents

Two enantiocomplementary Baeyer-Villiger monooxygenases newly identified for asymmetric oxyfunctionalization of thioether

Two enantiocomplementary Baeyer-Villiger monooxygenases RaBVMO and AmBVMO were identified by genome mining for the asymmetric sulfoxidation. Both recombinant BVMOs have optimal pH of 9.0 and temperature of 35 °C. The half-lives of RaBVMO and AmBVMO at 30 °C were 24.4 and 24.6 h. RaBVMO and AmBVMO exhibited broad substrate spectrum and could catalyze the oxidization of various compounds including fatty ketones, cyclic ketones, and thioethers. Kinetic parameters analysis revealed that both RaBVMO and AmBVMO displayed higher catalytic efficiency toward thioanisole than cyclohexanone. As much as 50 mM thioanisole could be completely oxidized by AmBVMO and RaBVMO with 99% (R) and 95% (S), respectively. Molecular docking analysis further provides evidence for the complementary enantioselectivity of RaBVMO and AmBVMO. Our results demonstrate the potential application of the two novel BVMOs in asymmetric synthesis of sulfoxides.

Chiral separation materials based on derivatives of 6-amino-6-deoxyamylose

In order to develop new type of chiral separation materials, in this study, 6-amino-6-deoxyamylose was used as chiral starting material with which 10 derivatives were synthesized. The amino group in 6-amino-6-deoxyamylose was selectively acylated and then the hydroxyl groups were carbamoylated yielding amylose 6-amido-6-deoxy-2,3-bis(phenylcarbamate)s, which were employed as chiral selectors (CSs) for chiral stationary phases of high-performance liquid chromatography. The resulted 6-amido-6-deoxyamyloses and amylose 6-amido-6-deoxy-2,3-bis(phenylcarbamate)s were characterized by IR, 1H NMR, and elemental analysis. Enantioseparation evaluations indicated that most of the CSs demonstrated a moderate chiral recognition capability. The 6-nonphenyl (6-nonPh) CS of amylose 6-cyclohexylformamido-6-deoxy-2,3-bis(3,5-dimethylphenylcarbamate) showed the highest enantioselectivity towards the tested chiral analytes; the phenyl-heterogeneous (Ph-hetero) CS of amylose 6-(4-methylbenzamido)-6-deoxy-2,3-bis(3,5-dimethylphenylcarbamate) baseline separated the most chiral analytes; the phenyl-homogeneous (Ph-homo) CS of amylose 6-(3,5-dimethylbenzamido)-6-deoxy-2,3-bis(3,5-dimethylphenylcarbamate) also exhibited a good enantioseparation capability among the developed CSs. Regarding Ph-hetero CSs, the enantioselectivity depended on the combination of the substituent at 6-position and that at 2- and 3-positions; as for Ph-homo CSs, the enantioselectivity was related to the substituent at 2-, 3-, and 6-positions; with respect to 6-nonPh CSs, the retention factor of most analytes on the corresponding CSPs was lower than that on Ph-hetero and Ph-homo CSPs in the same mobile phases, indicating π–π interactions did occur during enantioseparation. Although the substituent at 6-position could not provide π–π interactions, the 6-nonPh CSs demonstrated an equivalent or even higher enantioselectivity compared with the Ph-homo and Ph-hetero CSs.

Chiral: N, N ′-dioxide-iron(iii)-catalyzed asymmetric sulfoxidation with hydrogen peroxide

A highly enantioselective sulfoxidation of various sulfides has been achieved by a N,N′-dioxide-iron(iii) complex with 35% aq. H2O2 as the oxidant. The utility of the current method was demonstrated by asymmetric gram-scale synthesis of drug molecule (R)-modafinil. Moreover, a possible working mode was provided to elucidate the chiral induction.

Discovery and application of methionine sulfoxide reductase B for preparation of (S)-sulfoxides through kinetic resolution

Here we report a methionine sulfoxide reductase B (MsrB) enzymatic system for the preparation of (S)-sulfoxides through kinetic resolution of racemic (rac) sulfoxides. Eight MsrB homologue recombinant proteins were expressed and their activities on asymmetric reduction of rac-sulfoxides were analyzed. Among these MsrB homologue proteins, one protein from Acidovorax species showed good activity and enantioselectivity towards several aryl-alkyl sulfoxides. The (S)-sulfoxides were prepared with 93–98% enantiomeric excess through kinetic resolution at initial substrate concentration up to 50 mM. The establishment of MsrB catalytic kinetic resolution system provides a new efficient green strategy for preparation of (S)-sulfoxides.

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.

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.

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).

Identification of MsrA homologues for the preparation of (R)-sulfoxides at high substrate concentrations

Here we report a methionine sulfoxide reductase A (MsrA) homologue with extremely high substrate tolerance and a wide substrate scope for the biocatalytic preparation of enantiopure sulfoxides. This MsrA homologue which was obtained from Pseudomonas alcaliphila (named paMsrA) showed good activity and enantioselectivity towards a series of aryl methyl/ethyl sulfoxides 1a-1k, with electron-withdrawing or electron-donating substituents at the aromatic ring. Chiral sulfoxides in the R configuration were prepared with approximately 50% of yield and up to 99% enantiomeric excess through the asymmetric reductive resolution of racemic sulfoxide catalyzed by the recombinant paMsrA protein. More importantly, kinetic resolution has been successfully accomplished with high enantioselectivity (E > 200) at initial substrate concentrations up to 320 mM (approximately 45 g L-1), which represents a great improvement in the aspect of the substrate concentration for the biocatalytic preparation of chiral sulfoxides.

Asymmetric sulfoxidation by C1-symmetric V(IV)O(ONO) (S)-NOBIN Schiff-base vanadyl complexes

C1-symmetric vanadyl Schiff-base complexes were synthesized by reacting vanadium(IV) acetylacetonate with (S)-3-[(1-(2-hydroxynaphthalen-1-yl)naphthalen-2-ylimino]methyl]-phenanthrene-4-ol and (S)-2-{[1-(2-hydroxynaphthalen-1-yl)naphthalen-2-ylimino]methyl}tetraphene-1-ol. The complexes were characterized by MALDI-TOF-MS, UV-vis, and circular dichroism (CD) spectroscopy. The catalysts showed moderate activity for the oxidation of thioanisole to methyphenylsulfoxide with hydrogen peroxide, tert-butyl hydroperoxide, and cumene hydroperoxide as the oxidants.

Enhanced Activity and Substrate Specificity by Site-Directed Mutagenesis for the P450 119 Peroxygenase Catalyzed Sulfoxidation of Thioanisole

P450 119 peroxygenase was found to catalyze the sulfoxidation of thioanisole and the sulfonation of sulfoxide in the presence of tert-butyl hydroperoxide (TBHP) for the first time with turnover rates of 1549 min?1 and 196 min?1 respectively. Several mutants were designed to improve the peroxygenation activity and thioanisole specificity by site-directed mutagenesis. The F153G/T213G mutant gave an increase of sulfoxide yield and a decrease of sulfone yield. Moreover the S148P/I161T/K199E/T214V mutant and the K199E mutant with acidic Glu residue contributed to improving the product ratio of sulfoxide to sulfone. Addition of short-alkyl-chain organic acids to the P450 119 peroxygenase-catalyzed sulfur oxidation of thioanisole was investigated. Octanoic acid was found to induce a preferred sulfoxidation of thioanisole catalyzed by the F153G/T213G mutant to give approximately 2.4-fold increase in turnover rate with a kcat value of 3687 min?1 relative to that of the wild-type, and by the F153G mutant to give the R-sulfoxide up to 30 % ee. The experimental control and the proposed mechanism for the P450 119 peroxygenase-catalyzed sulfoxidation of thioanisole in the presence of octanoic acid suggested that octanoic acid could partially occupy the substrate pocket; meanwhile the F153G mutation could enhance the substrate specificity, which could lead to efficiently regulate the spatial orientation of thioanisole and facilitate the formation of Compound I. This is the most effective catalytic system for the P450 119 peroxygenase-catalyzed sulfoxidation of thioanisole.