Difference between revisions of "Hildebrandt 2008 FEBS J"
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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. FEBS J | |title=Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275:3352-6. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18494801 PMID: 18494801] | |||
|authors=Hildebrandt TM, Grieshaber MK | |authors=Hildebrandt TM, Grieshaber MK | ||
|year=2008 | |year=2008 | ||
|journal=FEBS J | |journal=FEBS J | ||
|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. | |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 | |keywords=Mitochondria, Sulfide oxidation, Sulfide : quinone oxidoreductase, Sulfur dioxygenase, Sulfur transferase | ||
| | |mipnetlab=DE Duesseldorf Grieshaber MK, DE Hannover Hildebrandt T | ||
|discipline=Mitochondrial Physiology, Pharmacology; Biotechnology | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration, Comparative MiP;environmental MiP | |||
|injuries=Ischemia-reperfusion | |||
|organism=Rat, Annelids | |||
|tissues=Liver | |||
|preparations=Isolated mitochondria | |||
|topics=Inhibitor, Substrate | |||
|couplingstates=OXPHOS | |||
|instruments=Oxygraph-2k | |||
|additional=Sulfide | |||
|discipline=Mitochondrial Physiology, Pharmacology; Biotechnology | |discipline=Mitochondrial Physiology, Pharmacology; Biotechnology | ||
}} | }} | ||
Latest revision as of 10:53, 27 March 2018
| Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275:3352-6. |
Hildebrandt TM, Grieshaber MK (2008) FEBS J
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
• O2k-Network Lab: DE Duesseldorf Grieshaber MK, DE Hannover Hildebrandt T
Labels: MiParea: Respiration, Comparative MiP;environmental MiP
Stress:Ischemia-reperfusion Organism: Rat, Annelids Tissue;cell: Liver Preparation: Isolated mitochondria
Regulation: Inhibitor, Substrate Coupling state: OXPHOS
HRR: Oxygraph-2k
Sulfide
