The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Sulfanol     sulfanol

Synonyms: HSOH, Sulfensaeure, sulphenic acid, sulfenic acid, AGN-PC-0CPMPJ, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of sulfanol


High impact information on sulfanol


Biological context of sulfanol

  • This is further supported by the absence of sequence homology between the two Msrs in particular around the cysteine that is involved in formation of the sulfenic acid derivative [9].
  • Instead, multiple cysteines distributed in both the N-terminal substrate-binding domain (Cys147 in particular) and the C-terminal catalytic domain (Cys218) are capable of rapidly and efficiently trapping the sulfenic acid as a disulfide [10].
  • The reaction is supposed to occur as a result of intramolecular acyl transfer from Cys-149 to a sulfenic acid form of Cys-153, followed by hydrolysis of the intermediate [11].
  • In this paper, a new strategy is described, which makes use of beta-elimination/Michael addition reactions to introduce a functional group at the original site of phosphorylation, which gives rise to a dimethylamine-containing sulfenic acid derivative with a unique m/z value [12].

Associations of sulfanol with other chemical compounds


Gene context of sulfanol

  • The oxidized intermediate of PrxV is thus distinct from those of other Prx enzymes, which form either an intermolecular disulfide or a sulfenic acid intermediate [18].
  • It was first characterized for its regulation of Prx(s) through reduction of the conserved cysteine from sulfinic to sulfenic acid, thereby impacting the role of Prx in regulation of downstream transcription factors and kinase signaling pathways [19].
  • These findings suggest that nitric oxide inhibits GAPDH activity by modifications of the thiols which are essential for this activity, and that the modification includes formation of sulfenic acid, which is not restored by DTT [17].
  • Human flavin-containing monooxygenase form 2 S-oxygenation: sulfenic acid formation from thioureas and oxidation of glutathione [20].
  • This result demonstrates that the NOR-1-dependent formation of cathepsin K sulfinic and sulfonic acids occurs via a sulfenic acid [16].


  1. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., Branlant, G. J. Biol. Chem. (2000) [Pubmed]
  2. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Ellis, H.R., Poole, L.B. Biochemistry (1997) [Pubmed]
  3. Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303. Mande, S.S., Parsonage, D., Claiborne, A., Hol, W.G. Biochemistry (1995) [Pubmed]
  4. Structure, mechanism and regulation of peroxiredoxins. Wood, Z.A., Schröder, E., Robin Harris, J., Poole, L.B. Trends Biochem. Sci. (2003) [Pubmed]
  5. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Monteiro, G., Horta, B.B., Pimenta, D.C., Augusto, O., Netto, L.E. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  6. Redox activation of aldose reductase in the ischemic heart. Kaiserova, K., Srivastava, S., Hoetker, J.D., Awe, S.O., Tang, X.L., Cai, J., Bhatnagar, A. J. Biol. Chem. (2006) [Pubmed]
  7. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. Baker, L.M., Poole, L.B. J. Biol. Chem. (2003) [Pubmed]
  8. Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., Lunardi, J. J. Biol. Chem. (2002) [Pubmed]
  9. Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis. Olry, A., Boschi-Muller, S., Marraud, M., Sanglier-Cianferani, S., Van Dorsselear, A., Branlant, G. J. Biol. Chem. (2002) [Pubmed]
  10. Redox regulation of MAP kinase phosphatase 3. Seth, D., Rudolph, J. Biochemistry (2006) [Pubmed]
  11. Rabbit muscle GAPDH: non-phosphorylating dehydrogenase activity induced by hydrogen peroxide. Schmalhausen, E.V., Muronetz, V.I., Nagradova, N.K. FEBS Lett. (1997) [Pubmed]
  12. A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode. Steen, H., Mann, M. J. Am. Soc. Mass Spectrom. (2002) [Pubmed]
  13. How does alendronate inhibit protein-tyrosine phosphatases? Skorey, K., Ly, H.D., Kelly, J., Hammond, M., Ramachandran, C., Huang, Z., Gresser, M.J., Wang, Q. J. Biol. Chem. (1997) [Pubmed]
  14. Identification and localization of a stable sulfenic acid in peroxide-treated tetrachlorohydroquinone dehalogenase using electrospray mass spectrometry. Willett, W.S., Copley, S.D. Chem. Biol. (1996) [Pubmed]
  15. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Denu, J.M., Tanner, K.G. Biochemistry (1998) [Pubmed]
  16. Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Percival, M.D., Ouellet, M., Campagnolo, C., Claveau, D., Li, C. Biochemistry (1999) [Pubmed]
  17. Critical role of sulfenic acid formation of thiols in the inactivation of glyceraldehyde-3-phosphate dehydrogenase by nitric oxide. Ishii, T., Sunami, O., Nakajima, H., Nishio, H., Takeuchi, T., Hata, F. Biochem. Pharmacol. (1999) [Pubmed]
  18. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. Seo, M.S., Kang, S.W., Kim, K., Baines, I.C., Lee, T.H., Rhee, S.G. J. Biol. Chem. (2000) [Pubmed]
  19. Sulfiredoxin: a potential therapeutic agent? Findlay, V.J., Tapiero, H., Townsend, D.M. Biomed. Pharmacother. (2005) [Pubmed]
  20. Human flavin-containing monooxygenase form 2 S-oxygenation: sulfenic acid formation from thioureas and oxidation of glutathione. Henderson, M.C., Krueger, S.K., Stevens, J.F., Williams, D.E. Chem. Res. Toxicol. (2004) [Pubmed]
WikiGenes - Universities