S-Nitrosation of Conserved Cysteines Modulates Activity and Stability of S-Nitrosoglutathione Reductase (GSNOR).

@article{Guerra2016SNitrosationOC,
  title={S-Nitrosation of Conserved Cysteines Modulates Activity and Stability of S-Nitrosoglutathione Reductase (GSNOR).},
  author={Damian D. Guerra and Keith Ballard and Ian Truebridge and Elizabeth Vierling},
  journal={Biochemistry},
  year={2016},
  volume={55 17},
  pages={2452-64}
}
The free radical nitric oxide (NO(•)) regulates diverse physiological processes from vasodilation in humans to gas exchange in plants. S-Nitrosoglutathione (GSNO) is considered a principal nitroso reservoir due to its chemical stability. GSNO accumulation is attenuated by GSNO reductase (GSNOR), a cysteine-rich cytosolic enzyme. Regulation of protein nitrosation is not well understood since NO(•)-dependent events proceed without discernible changes in GSNOR expression. Because GSNORs contain… CONTINUE READING
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Cysteine sulfur

  • J. L. Luebke, D. P. Giedroc
  • 2015

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