Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway
Sulfide oxidation is expected to play an important role in cellular switching between low steady-state intracellular hydrogen sulfide levels and the higher concentrations where the physiological effects are elicited. Yet despite its significance, fundamental questions regarding how the sulfide oxida...
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| Veröffentlicht in: | The Journal of biological chemistry 2014-11, Vol.289 (45), p.30901-30910 |
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| container_title | The Journal of biological chemistry |
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| creator | Libiad, Marouane Yadav, Pramod Kumar Vitvitsky, Victor Martinov, Michael Banerjee, Ruma |
| description | Sulfide oxidation is expected to play an important role in cellular switching between low steady-state intracellular hydrogen sulfide levels and the higher concentrations where the physiological effects are elicited. Yet despite its significance, fundamental questions regarding how the sulfide oxidation pathway is wired remain unanswered, and competing proposals exist that diverge at the very first step catalyzed by sulfide quinone oxidoreductase (SQR). We demonstrate that, in addition to sulfite, glutathione functions as a persulfide acceptor for human SQR and that rhodanese preferentially synthesizes rather than utilizes thiosulfate. The kinetic behavior of these enzymes provides compelling evidence for the flow of sulfide via SQR to glutathione persulfide, which is then partitioned to thiosulfate or sulfite. Kinetic simulations at physiologically relevant metabolite concentrations provide additional support for the organizational logic of the sulfide oxidation pathway in which glutathione persulfide is the first intermediate formed. |
| doi_str_mv | 10.1074/jbc.M114.602664 |
| format | Article |
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Yet despite its significance, fundamental questions regarding how the sulfide oxidation pathway is wired remain unanswered, and competing proposals exist that diverge at the very first step catalyzed by sulfide quinone oxidoreductase (SQR). We demonstrate that, in addition to sulfite, glutathione functions as a persulfide acceptor for human SQR and that rhodanese preferentially synthesizes rather than utilizes thiosulfate. The kinetic behavior of these enzymes provides compelling evidence for the flow of sulfide via SQR to glutathione persulfide, which is then partitioned to thiosulfate or sulfite. Kinetic simulations at physiologically relevant metabolite concentrations provide additional support for the organizational logic of the sulfide oxidation pathway in which glutathione persulfide is the first intermediate formed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M114.602664</identifier><identifier>PMID: 25225291</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Catalysis ; Cysteine - chemistry ; Cytochromes c - chemistry ; Enzymology ; Escherichia coli - enzymology ; Glutathione - chemistry ; Homeostasis ; Humans ; Hydrogen Sulfide - chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Mitochondria - metabolism ; Oxidation-Reduction ; Oxygen - chemistry ; Quinone Reductases - chemistry ; Spectrophotometry, Ultraviolet ; Sulfides - chemistry ; Thiosulfate Sulfurtransferase - chemistry</subject><ispartof>The Journal of biological chemistry, 2014-11, Vol.289 (45), p.30901-30910</ispartof><rights>2014 © 2014 ASBMB. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Catalysis Cysteine - chemistry Cytochromes c - chemistry Enzymology Escherichia coli - enzymology Glutathione - chemistry Homeostasis Humans Hydrogen Sulfide - chemistry Hydrogen-Ion Concentration Kinetics Mitochondria - metabolism Oxidation-Reduction Oxygen - chemistry Quinone Reductases - chemistry Spectrophotometry, Ultraviolet Sulfides - chemistry Thiosulfate Sulfurtransferase - chemistry |
| title | Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway |
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