Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed? Free Radic Biol Med 2010 Jan 01;48(1):55-64
Date
10/13/2009Pubmed ID
19819329Pubmed Central ID
PMC2829852DOI
10.1016/j.freeradbiomed.2009.10.026Scopus ID
2-s2.0-74049084627 (requires institutional sign-in at Scopus site) 143 CitationsAbstract
The reaction between NO, thiols, and oxygen has been studied in some detail in vitro due to its perceived importance in the mechanism of NO-dependent signal transduction. The formation of S-nitrosothiols and thiol disulfides from this chemistry has been suggested to be an important component of the biological chemistry of NO, and such subsequent thiol modifications may result in changes in cellular function and phenotype. In this study we have reinvestigated this reaction using both experiment and simulation and conclude that: (i) S-nitrosation through radical and nonradical pathways is occurring simultaneously, (ii) S-nitrosation through direct addition of NO to thiol does not occur to any meaningful extent, and (iii) protein hydrophobic environments do not catalyze or enhance S-nitrosation of either themselves or of glutathione. We conclude that S-nitrosation and disulfide formation in this system occur only after the initial reaction between NO and oxygen to form nitrogen dioxide, and that hydrophobic protein environments are unlikely to play any role in enhancing and targeting S-nitrosothiol formation.
Author List
Keszler A, Zhang Y, Hogg NAuthors
Neil Hogg PhD Senior Associate Dean, Professor in the Biophysics department at Medical College of WisconsinAgnes Keszler Research Scientist I in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnimalsCattle
Glutathione
Humans
Kinetics
Nitric Oxide
Oxidation-Reduction
Oxygen
S-Nitrosothiols
Serum Albumin
Time Factors
