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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1997-1-16
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pubmed:abstractText |
The S-nitroso adducts of nitric oxide (NO) may serve as carriers of NO and play a role in cell signaling and/or cytotoxicity. A quantitative understanding of the kinetics of S-nitrosothiol formation in solutions containing NO and O2 is important for understanding these roles of S-nitroso compounds in vivo. Rates of S-nitrosation in aqueous solutions were investigated for three thiols: glutathione, N-acetylcysteine, and N-acetylpenicillamine. Nitrous anhydride (N2O3), an intermediate in the formation of nitrite from NO and O2, is the most likely NO donor for N-nitrosation of amines as well as for S-nitrosation of thiols, at physiological pH. This motivated the use of a competitive kinetics approach, in which the rates of thiol nitrosation were compared with that of a secondary amine, morpholine. The kinetic studies were carried out with known amounts of NO and O2 in solutions containing one thiol (400 microM) and morpholine (200-5700 microM) in 0.01 M phosphate buffer at pH 7.4 and 23 degrees C. It was found that disulfide formation, transnitrosation reactions, and decomposition of the S-nitrosothiols was expressed as k7[N2O3][RSH], where RSH represents the thiol. The rate constant for S-nitrosation relative to that for N2O3 hydrolysis (k4) was found to be k7/k4 = (4.15 +/- 0.28) x 10(4), (2.11 +/- 0.11) x 10(4), and (0.48 +/- 0.04) x 10(4) M-1 for glutathione, N-acetylcysteine, and N-acetylpenicillamine, respectively. The overall (observed) rates of nitrosothiol formation reflect the fact that [N2O3] varies [NO]2[O2] and that [N2O3] also depends on [RSH] and the concentration of phosphate. Using a detailed kinetic model to account for these effects, the present results could be reconciled with apparently dissimilar findings reported previously by others.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Morpholines,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen Oxides,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/morpholine,
http://linkedlifedata.com/resource/pubmed/chemical/nitrogen trioxide
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0893-228X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
988-93
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8870986-Acetylcysteine,
pubmed-meshheading:8870986-Glutathione,
pubmed-meshheading:8870986-Kinetics,
pubmed-meshheading:8870986-Morpholines,
pubmed-meshheading:8870986-Nitric Oxide,
pubmed-meshheading:8870986-Nitrogen Oxides,
pubmed-meshheading:8870986-Nitrosation,
pubmed-meshheading:8870986-Solutions,
pubmed-meshheading:8870986-Sulfhydryl Compounds
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pubmed:year |
1996
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pubmed:articleTitle |
Kinetics of S-nitrosation of thiols in nitric oxide solutions.
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pubmed:affiliation |
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge 02139, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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