Redox Biochemistry of Hydrogen Sulfide*
By O. Kabil, R. Banerjee. Journal of Biological Chemistry, 2010
698 citations recorded by the source corpus.
H2S, the most recently discovered gasotransmitter, might in fact be the evolutionary matriarch of this family, being both ancient and highly reduced. Disruption of γ-cystathionase in mice leads to cardiovascular dysfunction and marked hypertension, suggesting a key role for this enzyme in H2S production in the vasculature. However, patients with inherited deficiency in γ-cystathionase apparently do not present vascular pathology. A mitochondrial pathway disposes sulfide and couples it to oxidative phosphorylation while also exposing cytochrome c oxidase to this metabolic poison. This report focuses on the biochemistry of H2S biogenesis and clearance, on the molecular mechanisms of its action, and on its varied biological effects.
Subfields: Biochemistry, Molecular Biology, Rheumatology
View Paper: https://www.semanticscholar.org/paper/1e17145f98ca720adb9fbddeea7012c7ac0b5756
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In Biochemistry
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Citations in the corpus
- Physiological implications of hydrogen sulfide: a whiff exploration that blossomed. (2012, background): “The former requires the presence of reductants (288) and the latter, specific enzymes such as thiosulfate sulfurtransferase or thiosulfate reductase (599).”
- The thiol pool in human plasma: The central contribution of albumin to redox processes (2013, background): “Hydrogen sulfide is synthesized mainly as a by-product of the transsulfuration enzymes that catalize the formation of cysteine from methionine and is catabolized principally in the mitochondria (for review see [13]).”
- Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling (2014, positive): “Although previous reports describe H2S as a major signaling molecule in mammals (1, 9), results herein suggest that the Cysbased persulfides may be the actual signaling species.”