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Chemical Compound Review

Thioanisol     methylsulfanylbenzene

Synonyms: PHSME, Thioanisole, SureCN7584, PubChem10578, AGN-PC-008LG3, ...
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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


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].


  1. On the formation and reactivity of compound I of the His-64 myoglobin mutants. Matsui, T., Ozaki, S., Watanabe, Y. J. Biol. Chem. (1997) [Pubmed]
  2. Molecular engineering of myoglobin: influence of residue 68 on the rate and the enantioselectivity of oxidation reactions catalyzed by H64D/V68X myoglobin. Yang, H.J., Matsui, T., Ozaki, S., Kato, S., Ueno, T., Phillips, G.N., Fukuzumi, S., Watanabe, Y. Biochemistry (2003) [Pubmed]
  3. A mechanistic study of the FeO+-mediated decomposition pathways of phenol, anisol, and their thio analogues. Brönstrup, M., Schröder, D., Schwarz, H. Chemistry (Weinheim an der Bergstrasse, Germany) (2000) [Pubmed]
  4. Transient-state kinetics of the reactions of 1-methoxy-4-(methylthio)benzene with horseradish peroxidase compounds I and II. Pérez, U., Dunford, H.B. Biochemistry (1990) [Pubmed]
  5. Synthesis of 2,3-disubstituted benzo[b]thiophenes via palladium-catalyzed coupling and electrophilic cyclization of terminal acetylenes. Yue, D., Larock, R.C. J. Org. Chem. (2002) [Pubmed]
  6. Solution-phase synthesis of an anti-human immunodeficiency virus peptide, T22 ([Tyr5,12,Lys7]-polyphemusin II), and the modification of Trp by the p-methoxybenzyl group of Cys during trimethylsilyl trifluoromethanesulfonate deprotection. Tamamura, H., Otaka, A., Takada, W., Terakawa, Y., Yoshizawa, H., Masuda, M., Ibuka, T., Murakami, T., Nakashima, H., Waki, M. Chem. Pharm. Bull. (1995) [Pubmed]
  7. Metabolism of 2,3,5,6-tetrachloronitrobenzene (tecnazene) in rat. Lappin, G.J., Pritchard, D., Moore, R.B., Laird, W.J. Xenobiotica (1996) [Pubmed]
  8. The activation of molecular oxygen by horseradish peroxidase with sodium sulfite. Ozaki, S., Watanabe, S., Hayasaka, S., Konuma, M. Chem. Commun. (Camb.) (2001) [Pubmed]
  9. Oxygenation of organosulfur compounds by peroxidases: evidence of an electron transfer mechanism for lactoperoxidase. Doerge, D.R. Arch. Biochem. Biophys. (1986) [Pubmed]
  10. Chloroperoxidase-catalyzed enantioselective oxidations in hydrophobic organic media. van de Velde, F., Bakker, M., van Rantwijk, F., Sheldon, R.A. Biotechnol. Bioeng. (2001) [Pubmed]
  11. Peroxidase-catalyzed asymmetric sulfoxidation in organic solvents versus in water. Dai, L., Klibanov, A.M. Biotechnol. Bioeng. (2000) [Pubmed]
  12. Studies on peptides. CXIII. Synthesis of the heptacosapeptide amide corresponding to the entire amino acid sequence of chicken secretin. Kiyama, S., Fujii, N., Yajima, H., Moriga, M., Takagi, A. Int. J. Pept. Protein Res. (1984) [Pubmed]
  13. The sulphoxidation of thioanisole catalysed by lactoperoxidase and Coprinus cinereus peroxidase: evidence for an oxygen-rebound mechanism. Tuynman, A., Vink, M.K., Dekker, H.L., Schoemaker, H.E., Wever, R. Eur. J. Biochem. (1998) [Pubmed]
  14. New aspects of the reactivity of tyrosinase. Casella, L., Granata, A., Monzani, E., Pievo, R., Pattarello, L., Bubacco, L. Micron (2004) [Pubmed]
  15. Side-chain deprotection of peptides synthesized onto a beaded cellulose support. Englebretsen, D.R., Harding, D.R. Pept. Res. (1994) [Pubmed]
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