High impact information on methylsulfanylbenzene

• Furthermore, Mb-I is found to be capable of performing two-electron oxidation of styrene, thioanisole, and H2O2 [1].
• However, comparison of the active site structures provides the basis to interpret the changes in oxidation activity: (1) direct steric interactions between residue 68 and substrates (i.e., H(2)O(2), ABTS, thioanisole) and (2) the polar interactions between tightly hydrogen-bonded water molecules and substrates [2].
• For anisol and thioanisol, analogies and differences between oxidation reactions catalyzed by the enzyme cytochrome P-450 in the condensed phase and those observed for the gas-phase model FeO+ are discussed [3].
• Transient-state reactions of horseradish peroxidase compounds I and II with 1-methoxy-4-(methylthio)benzene (a para-substituted thioanisole) were studied over the pH range from 3.4 to 10 [4].
• However, cyclization of the silyl-containing thioanisole using Br(2) affords 2,3-dibromobenzo[b]thiophene [5].

Biological context of methylsulfanylbenzene

• An 18-residue peptide amide corresponding to the entire amino acid sequence of T22 was synthesized by assembling four peptide fragments and two amino acid derivatives, followed by thioanisole-mediated deprotection with 1 M trimethylsilyl trifluoromethanesulfonate (TMSOTf) in trifluoroacetic acid followed by air-oxidation [6].
• The cysteine conjugate underwent beta-lyase-mediated metabolism to yield a thiol that underwent subsequent methylation to the thioanisole followed by S-oxidation [7].

Associations of methylsulfanylbenzene with other chemical compounds

• Horseradish peroxidase (HRP) utilizes molecular oxygen (O2) with sodium sulfite (Na2SO3) to oxidize thioanisole and styrene at the exterior of the heme pocket [8].
• The oxygenation of benzyl methylsulfide, thioanisole, and thiobenzamide to the respective sulfoxides was found to be catalyzed by chloroperoxidase, lactoperoxidase, and horseradish peroxidase [9].
• Thioanisole was converted into the corresponding (R)-sulfoxide (ee > 99%) in isooctane medium.The complexes of CPO with sodium octadecylsulphate or ethyl cellulose mediated the oxidation of thioanisole in water-immiscible organic media with variable enantioselectivity due to radical side-reactions [10].
• Sulfoxidation of thioanisole catalyzed by four other hemoproteins (soybean peroxidase, myoglobin, hemoglobin, and cytochrome c) is also much faster in isopropyl alcohol than in water [11].
• The heptacosapeptide amide corresponding to the entire amino acid sequence of chicken secretin was synthesized by assembling four peptide fragments followed by deprotection with thioanisole-mediated trifluoromethanesulfonic acid in TFA [12].

Gene context of methylsulfanylbenzene

• The sulphoxidation of thioanisole catalysed by lactoperoxidase and Coprinus cinereus peroxidase: evidence for an oxygen-rebound mechanism [13].
• Tyrosinase was found to be active in the sulfoxidation of thioanisol, producing the (R)-sulfoxide with high enantiomeric excess [14].
• A cocktail of m-cesol/EDT/thioanisole/TMSBr/TFA/DCM (1:1:2:2:15:79 by volume-Reagent D) was found to cleave amino acid side-chain-protecting groups while leaving the chromatographic properties of the peptide-resin unaltered [15].

References