Laboratoire de Bioénergétique et Ingénierie des Protéines, IMM-CNRS, 31 chemin Joseph Aiguier, Marseille cedex 20, France.
Biochimie. 2010 Apr;92(4):388-97. doi: 10.1016/j.biochi.2009.12.013. Epub 2010 Jan 8.
Rhodaneses (thiosulfate cyanide sulfurtransferases) are enzymes involved in the production of the sulfur in sulfane form, which has been suggested to be the relevant biologically active sulfur species. Rhodanese domains occur in the three major domains of life. We have characterized a new periplasmic single-domain rhodanese from a hyperthermophile bacterium, Aquifex aeolicus, with thiosulfate:cyanide transferase activity, Aq-1599. The oligomeric organization of the enzyme is stabilized by a disulfide bridge. To date this is the first characterization from a hyperthermophilic bacterium of a periplasmic sulfurtransferase with a disulfide bridge. The aq-1599 gene belongs to an operon that also contains a gene for a prepilin peptidase and that is up-regulated when sulfur is used as electron acceptor. Finally, we have observed a sulfur-dependent bacterial adherence linked to an absence of flagellin suggesting a possible role for sulfur detection by A. aeolicus.
硫氰酸盐转硫酶（Rhodaneses）是参与生成硫代硫酸根形式硫的酶，该硫代硫酸根形式的硫被认为是相关的具有生物活性的硫物种。硫氰酸盐转硫酶结构域存在于生命的三个主要领域。我们从一种嗜热菌 Aquifex aeolicus 中鉴定出一种新的周质单结构域硫氰酸盐转硫酶 Aq-1599，该酶具有硫代硫酸盐：氰化物转移酶活性。酶的寡聚体组织由二硫键稳定。迄今为止，这是首次从嗜热菌中鉴定出具有二硫键的周质硫转移酶。aq-1599 基因属于一个操纵子，该操纵子还包含一个前导肽酶基因，当硫作为电子受体时，该操纵子被上调。最后，我们观察到一种与鞭毛蛋白缺失相关的硫依赖性细菌黏附，这表明 A. aeolicus 可能具有硫检测的功能。
