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Antioxid Redox Signal. 2014 Feb 10;20(5):770-82. doi: 10.1089/ars.2013.5339. Epub 2013 Jun 7.

Enzymology of H2S biogenesis, decay and signaling.

Author information

1
Department of Biological Chemistry, University of Michigan Medical School , Ann Arbor, Michigan.

Abstract

SIGNIFICANCE:

Hydrogen sulfide (H2S), produced by the desulfuration of cysteine or homocysteine, functions as a signaling molecule in an array of physiological processes including regulation of vascular tone, the cellular stress response, apoptosis, and inflammation.

RECENT ADVANCES:

The low steady-state levels of H2S in mammalian cells have been recently shown to reflect a balance between its synthesis and its clearance. The subversion of enzymes in the cytoplasmic trans-sulfuration pathway for producing H2S from cysteine and/or homocysteine versus producing cysteine from homocysteine, presents an interesting regulatory problem.

CRITICAL ISSUES:

It is not known under what conditions the enzymes operate in the canonical trans-sulfuration pathway and how their specificity is switched to catalyze the alternative H2S-producing reactions. Similarly, it is not known if and whether the mitochondrial enzymes, which oxidize sulfide and persulfide (or sulfane sulfur), are regulated to increase or decrease H2S or sulfane-sulfur pools.

FUTURE DIRECTIONS:

In this review, we focus on the enzymology of H2S homeostasis and discuss H2S-based signaling via persulfidation and thionitrous acid.

PMID:
23600844
PMCID:
PMC3910450
DOI:
10.1089/ars.2013.5339
[Indexed for MEDLINE]
Free PMC Article

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