Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria

authored by: Tatjana M. Hildebrandt, Manfred K. Grieshaber
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.
External Organisation(s): University Hospital Düsseldorf
Type: Article
Journal: FEBS Journal
Volume: 275
Pages: 3352-3361
No. of pages: 10
ISSN: 1742-464X
Publication date: 07.2008
Publication status: Published
Peer reviewed: Yes
ASJC Scopus subject areas: Biochemistry, Molecular Biology, Cell Biology
Electronic version(s): https://doi.org/10.1111/j.1742-4658.2008.06482.x (Access: Open)

BibTeX

@article{5bedec7b02d74e82b2ed9b927419b1b5,
title = "Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria",
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",
author = "Hildebrandt, {Tatjana M.} and Grieshaber, {Manfred K.}",
year = "2008",
month = jul,
doi = "10.1111/j.1742-4658.2008.06482.x",
language = "English",
volume = "275",
pages = "3352--3361",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "John Wiley and Sons Inc.",
number = "13",
}