Details
| Original language | English |
|---|---|
| Pages (from-to) | 3352-3361 |
| Number of pages | 10 |
| Journal | FEBS Journal |
| Volume | 275 |
| Issue number | 13 |
| Publication status | Published - Jul 2008 |
| Externally published | Yes |
Abstract
Hydrogen sulfide is a potent toxin of aerobic respiration, but also has physiological functions as a signalling molecule and as a substrate for ATP production. A mitochondrial pathway catalyzing sulfide oxidation to thiosulfate in three consecutive reactions has been identified in rat liver as well as in the body-wall tissue of the lugworm, Arenicola marina. A membrane-bound sulfide: quinone oxidoreductase converts sulfide to persulfides and transfers the electrons to the ubiquinone pool. Subsequently, a putative sulfur dioxygenase in the mitochondrial matrix oxidizes one persulfide molecule to sulfite, consuming molecular oxygen. The final reaction is catalyzed by a sulfur transferase, which adds a second persulfide from the sulfide: quinone oxidoreductase to sulfite, resulting in the final product thiosulfate. This role in sulfide oxidation is an additional physiological function of the mitochondrial sulfur transferase, rhodanese.
Keywords
- Mitochondria, Sulfide oxidation, Sulfide: quinone oxidoreductase, Sulfur dioxygenase, Sulfur transferase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS Journal, Vol. 275, No. 13, 07.2008, p. 3352-3361.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
AU - Hildebrandt, Tatjana M.
AU - Grieshaber, Manfred K.
PY - 2008/7
Y1 - 2008/7
N2 - Hydrogen sulfide is a potent toxin of aerobic respiration, but also has physiological functions as a signalling molecule and as a substrate for ATP production. A mitochondrial pathway catalyzing sulfide oxidation to thiosulfate in three consecutive reactions has been identified in rat liver as well as in the body-wall tissue of the lugworm, Arenicola marina. A membrane-bound sulfide: quinone oxidoreductase converts sulfide to persulfides and transfers the electrons to the ubiquinone pool. Subsequently, a putative sulfur dioxygenase in the mitochondrial matrix oxidizes one persulfide molecule to sulfite, consuming molecular oxygen. The final reaction is catalyzed by a sulfur transferase, which adds a second persulfide from the sulfide: quinone oxidoreductase to sulfite, resulting in the final product thiosulfate. This role in sulfide oxidation is an additional physiological function of the mitochondrial sulfur transferase, rhodanese.
AB - Hydrogen sulfide is a potent toxin of aerobic respiration, but also has physiological functions as a signalling molecule and as a substrate for ATP production. A mitochondrial pathway catalyzing sulfide oxidation to thiosulfate in three consecutive reactions has been identified in rat liver as well as in the body-wall tissue of the lugworm, Arenicola marina. A membrane-bound sulfide: quinone oxidoreductase converts sulfide to persulfides and transfers the electrons to the ubiquinone pool. Subsequently, a putative sulfur dioxygenase in the mitochondrial matrix oxidizes one persulfide molecule to sulfite, consuming molecular oxygen. The final reaction is catalyzed by a sulfur transferase, which adds a second persulfide from the sulfide: quinone oxidoreductase to sulfite, resulting in the final product thiosulfate. This role in sulfide oxidation is an additional physiological function of the mitochondrial sulfur transferase, rhodanese.
KW - Mitochondria
KW - Sulfide oxidation
KW - Sulfide: quinone oxidoreductase
KW - Sulfur dioxygenase
KW - Sulfur transferase
UR - http://www.scopus.com/inward/record.url?scp=44949214775&partnerID=8YFLogxK
U2 - 10.1111/j.1742-4658.2008.06482.x
DO - 10.1111/j.1742-4658.2008.06482.x
M3 - Article
C2 - 18494801
AN - SCOPUS:44949214775
VL - 275
SP - 3352
EP - 3361
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 13
ER -