Hildebrandt 2008 FEBS J: Difference between revisions
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{{Publication | {{Publication | ||
|title=Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. | |title=Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J. 275 (13):3352-61 | ||
|authors=Hildebrandt TM, Grieshaber MK | |authors=Hildebrandt TM, Grieshaber MK | ||
|year=2008 | |year=2008 | ||
|journal=The FEBS Journal | |||
|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 | |||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18494801 PMID: 18494801] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/18494801 PMID: 18494801] | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
| | |discipline=Mitochondrial Physiology, Pharmacology; Biotechnology | ||
|organism=Other Non-Mammal | |||
|kinetics=Inhibitor; Uncoupler | |||
|topics=Respiration; OXPHOS; ETS Capacity | |topics=Respiration; OXPHOS; ETS Capacity | ||
|instruments=Oxygraph-2k, Method | |||
|articletype=Protocol; Manual | |||
}} | }} | ||
Revision as of 16:21, 29 September 2010
| Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J. 275 (13):3352-61 |
Hildebrandt TM, Grieshaber MK (2008) The FEBS Journal
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
Labels:
Organism: Other Non-Mammal"Other Non-Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Regulation: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
HRR: Oxygraph-2k, Method"Method" is not in the list (Oxygraph-2k, TIP2k, O2k-Fluorometer, pH, NO, TPP, Ca, O2k-Spectrophotometer, O2k-Manual, O2k-Protocol, ...) of allowed values for the "Instrument and method" property.
