Sulfide inhibition of and metabolism by cytochrome c oxidase.

@article{Nicholls2013SulfideIO,
  title={Sulfide inhibition of and metabolism by cytochrome c oxidase.},
  author={Peter Nicholls and Doug Marshall and Chris E. Cooper and Mike T. Wilson},
  journal={Biochemical Society transactions},
  year={2013},
  volume={41 5},
  pages={
          1312-6
        }
}
  • Peter Nicholls, Doug Marshall, +1 author Mike T. Wilson
  • Published 2013
  • Chemistry, Medicine
  • Biochemical Society transactions
  • Hydrogen sulfide (H2S), a classic cytochrome c oxidase inhibitor, is also an in vitro oxidase substrate and an in vivo candidate hormonal ('gasotransmitter') species affecting sleep and hibernation. H2S, nitric oxide (NO) and carbon monoxide (CO) share some common features. All are low-molecular-mass physiological effectors and also oxidase inhibitors, capable of binding more than one enzyme site, and each is an oxidizable 'substrate'. The oxidase oxidizes CO to CO2, NO to nitrite and sulfide… CONTINUE READING

    Citations

    Publications citing this paper.
    SHOWING 1-10 OF 77 CITATIONS, ESTIMATED 29% COVERAGE

    Cytochrome bd and Gaseous Ligands in Bacterial Physiology.

    VIEW 2 EXCERPTS
    CITES BACKGROUND

    Hydrogen sulfide signaling in mitochondria and disease.

    Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology

    VIEW 28 EXCERPTS
    CITES BACKGROUND
    HIGHLY INFLUENCED

    FILTER CITATIONS BY YEAR

    2014
    2020

    CITATION STATISTICS

    • 3 Highly Influenced Citations

    • Averaged 14 Citations per year from 2018 through 2020

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 23 REFERENCES

    Oxidation of sulphide by cytochrome aa3.