Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

AC1LAVDQ 1-azanylidyne-N- (sulfanylidenemethylidene)...

Synonyms: isothiocyanato thiocyanate

Milligan, J.R. et al., Barnett, J.J. et al., Adak, S. et al., Adhikari, S. et al., Eadsforth, C.V. et al., et al.

Milligan, Aguilera, Mares, Paglinawan, Ward, Milligan, Aguilera, Ward,

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 Thiocyanogen

PURPOSE: Gamma irradiation of an aqueous solution containing thiocyanate ions produces the strongly oxidizing intermediate (SCN)2*-. Reaction of this species with plasmid DNA produces damage that is revealed as strand breaks after incubation with the Escherichia coli base excision repair endonuclease formamidopyrimidine-DNA N-glycosylase (FPG) [1].

High impact information on Thiocyanogen

The radicals dimerize to form thiocyanogen, (SCN)2, which is hydrolyzed to form CN-. As LPO forms OSCN- as the major stable oxidation product through a two-electron transfer mechanism, it is not significantly inactivated by CN- formed in a small quantity [2].
In the proposed mechanism, K(SCN)3(-) refers to the formation of (SCN)3(-) by association of SCN- with (SCN)2, K(hyd) refers to the hydrolysis of (SCN)2 to form HOSCN, and k(disp) is the rate constant for the bimolecular irreversible disproportionation of HOSCN, which leads ultimately to SO4(2-) and HCN [3].
PURPOSE: It has been previously argued that the use of the one-electron oxidants (SCN)2(*-) and Br2(*-) with plasmid DNA leads to the formation of DNA guanyl radicals [4].
Modification of the binding site by (Br)2- is independent of the initial concentration of Br-. Reaction of (SCN)2- with the protein, however, is dependent on the initial SCN- concentration [5].
The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin [6].

Analytical, diagnostic and therapeutic context of Thiocyanogen

Using the technique of pulse radiolysis, oxidation studies of the bovine serum albumin-bilirubin (BSA-BR) system with radicals like CCl3OO., N3., (SCN)2.-, Br2.- and OH. generated in neutral and alkaline medium are reported [7].

References

Redox equilibrium between guanyl radicals and thiocyanate influences base damage yields in gamma irradiated plasmid DNA. Estimation of the reduction potential of guanyl radicals in plasmid DNA in aqueous solution at physiological ionic strength. Milligan, J.R., Aguilera, J.A., Ward, J.F. Int. J. Radiat. Biol. (2001) [Pubmed]
Low catalytic turnover of horseradish peroxidase in thiocyanate oxidation. Evidence for concurrent inactivation by cyanide generated through one-electron oxidation of thiocyanate. Adak, S., Mazumdar, A., Banerjee, R.K. J. Biol. Chem. (1997) [Pubmed]
Acidic aqueous decomposition of thiocyanogen. Barnett, J.J., McKee, M.L., Stanbury, D.M. Inorganic chemistry. (2004) [Pubmed]
Reaction of guanyl radicals in plasmid DNA with biological reductants: chemical repair of DNA damage produced by the direct effect of ionizing radiation. Milligan, J.R., Aguilera, J.A., Mares, E.J., Paglinawan, R.A., Ward, J.F. Int. J. Radiat. Biol. (2001) [Pubmed]
Implication of tryptophan and tyrosine in the binding of p-nitrophenyl-alpha-D-mannopyranoside by concanavalin A. A radiolytic study. Moore, J.S., Mudher, S. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. (1979) [Pubmed]
Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2. Eadsforth, C.V., Power, D.M., Thomas, E.W. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. (1976) [Pubmed]
Oxidation reactions of a bovine serum albumin-bilirubin complex. A pulse radiolysis study. Adhikari, S., Gopinathan, C. Int. J. Radiat. Biol. (1996) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

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.