Dahl Christiane
Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany.
IUBMB Life. 2015 Apr;67(4):268-74. doi: 10.1002/iub.1371. Epub 2015 Apr 24.
Persulfide groups are chemically versatile and participate in a wide array of biochemical pathways. Although it is well documented that persulfurated proteins supply a number of important and elaborate biosynthetic pathways with sulfane sulfur, it is far less acknowledged that the enzymatic generation of persulfidic sulfur, the successive transfer of sulfur as a persulfide between multiple proteins, and the oxidation of sulfane sulfur in protein-bound form are also essential steps during dissimilatory sulfur oxidation in bacteria and archaea. Here, the currently available information on sulfur trafficking in sulfur oxidizing prokaryotes is reviewed, and the idea is discussed that sulfur is always presented to cytoplasmic oxidizing enzymes in a protein-bound form, thus preventing the occurrence of free sulfide inside of the prokaryotic cell. Thus, sulfur trafficking emerges as a central element in sulfur-oxidizing pathways, and TusA homologous proteins appear to be central and common elements in these processes.
过硫化物基团在化学性质上具有多样性，并参与多种生化途径。尽管有充分的文献记载，过硫化蛋白质为许多重要且复杂的生物合成途径提供硫烷硫，但人们对过硫化硫的酶促生成、硫作为过硫化物在多种蛋白质之间的连续转移以及蛋白质结合形式的硫烷硫的氧化在细菌和古菌异化硫氧化过程中也是必不可少的步骤却知之甚少。在此，对目前关于硫氧化原核生物中硫转运的可用信息进行了综述，并讨论了这样一种观点，即硫总是以蛋白质结合的形式呈现给细胞质氧化酶，从而防止原核细胞内游离硫化物的出现。因此，硫转运成为硫氧化途径的核心要素，而TusA同源蛋白似乎是这些过程中的核心且常见的要素。
