Hildebrandt 2008 FEBS J

Hildebrandt TM, Grieshaber MK (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria. FEBS J 275: 3352-3356.

» PMID: 18494801

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

Labels:

Organism: Rat  Tissue;cell: Liver 

Coupling state: OXPHOS 

HRR: Oxygraph-2k 

Sulfide