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Signaling through hydrogen sulfide
Author(s) -
Banerjee Ruma
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.528.4
Subject(s) - chemistry , hydrogen sulfide , sulfide , context (archaeology) , biochemistry , sulfur , biogenesis , enzyme , cystathionine beta synthase , cysteine , signal transduction , microbiology and biotechnology , biology , organic chemistry , gene , paleontology
Despite the excitement about the varied physiological effects mediated by H 2 S and the consequent profusion of literature on H 2 S biology, there are large gaps in our understanding of how cells maintain very low steady‐state levels of H 2 S and amplify the signal as needed (1). Three enzymes in the sulfur network are important for its biogenesis. Two catalyze well‐described non‐H 2 S producing reactions in the transsulfuration pathway and also synthesize cysteine persulfide from cystine (2), raising questions about how the decision between these competing reactions is made in the cell. The pathway for H 2 S oxidation resides in the mitochondrion where the enzymes successively oxidize sulfide to sulfate. While sulfate is innocuous, a number of the intermediates in the sulfide oxidation pathway are reactive and their role in sulfide‐based signaling remains to be assessed (3). We have recently discovered a noncanonical sulfide oxidation pathway (4, 5) and the challenging heme‐dependent oxidation chemistry will be discussed. We will also discuss how H 2 S signals via protein persulfidation in the context of cancer. Support or Funding Information This work was supported in part by the NIH (HL58984 and GM112455