PubMed · 4211914
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
S K Banerji. 1974. Detergents.. https://pubmed.ncbi.nlm.nih.gov/4211914/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
The objective of this study was to investigate the mechanism of S-nitrosothiol formation under physiological conditions. A mechanism is proposed by which nitric oxide (.NO) reacts directly with reduced thiol to produce a radical intermediate, R-S-N.-O-H. This intermediate reduces an electron acceptor to produce S-nitrosothiol. Under aerobic conditions O2 acts as the electron acceptor and is reduced to produce superoxide (O-2). The following experimental evidence is provided in support of this mechanism. Cysteine accelerates the consumption of .NO by 2.5-fold under physiological conditions. The consumption of O2 in the presence of .NO and cysteine is increased by 2.4-fold. The reaction orders of .NO and cysteine are second and first order, respectively. The second order of reaction for .NO may result from interaction between .NO and O-2 to form peroxynitrite. In the presence of Cu,Zn-superoxide dismutase, the reaction of .NO with cysteine generates hydrogen peroxide, indicating that the reaction generates O-2. Finally, the formation of S-nitrosothiol is demonstrated in an anaerobic environment and, as predicted by the mechanism, is dependent on the presence of an electron acceptor. These results demonstrate that under physiological conditions .NO reacts directly with thiols to form S-nitrosothiol in the presence of an electron acceptor.
SoxR is a [2Fe-2S] transcription factor triggered by oxidative stress and activated in vitro by one-electron oxidation or assembly of the iron-sulfur centers. To distinguish which mechanism operates in cells, we studied constitutively active SoxR (SoxRc) proteins. Three SoxRc proteins contained [2Fe-2S] centers required for in vitro transcription and, like wild-type SoxR, were inactivated by chemical reduction. However, in vivo spectroscopy showed that even without oxidative stress, the three SoxRc proteins failed to accumulate with reduced [2Fe-2S] (< or = 4% compared to > or = 40% for wild type). One SoxRc protein had a redox potential 65 mV lower than wild type, consistent with its accumulation in the oxidized (activated) form in vivo. These results link in vitro and in vivo approaches showing novel redox regulation that couples an iron-sulfur oxidation state to promoter activation.
Explore the source record for details and available documents.