Hildebrandt Tatjana M, Grieshaber Manfred K
Institut für Zoophysiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
FEBS J. 2008 Jul;275(13):3352-61. doi: 10.1111/j.1742-4658.2008.06482.x. Epub 2008 May 20.
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.
硫化氢是有氧呼吸的一种强效毒素，但它也具有作为信号分子和ATP生成底物的生理功能。在大鼠肝脏以及沙蠋（Arenicola marina）的体壁组织中，已鉴定出一条线粒体途径，该途径通过三个连续反应将硫化物氧化为硫代硫酸盐。一种膜结合的硫化物：醌氧化还原酶将硫化物转化为过硫化物，并将电子转移到泛醌池。随后，线粒体基质中的一种假定的硫双加氧酶将一个过硫化物分子氧化为亚硫酸盐，消耗分子氧。最终反应由硫转移酶催化，该酶将来自硫化物：醌氧化还原酶的第二个过硫化物添加到亚硫酸盐中，生成最终产物硫代硫酸盐。线粒体硫转移酶硫氰酸酶在硫化物氧化中的这一作用是其额外的生理功能。
