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Distribution, Diversity, and Activities of Sulfur Dioxygenases in Heterotrophic Bacteria

机译:异养细菌中硫双加氧酶的分布,多样性和活性

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Sulfur oxidation by chemolithotrophic bacteria is well known; however, sulfur oxidation by heterotrophic bacteria is often ignored. Sulfur dioxygenases (SDOs) (EC 1.13.11.18) were originally found in the cell extracts of some chemolithotrophic bacteria as glutathione (GSH)-dependent sulfur dioxygenases. GSH spontaneously reacts with elemental sulfur to generate glutathione persulfide (GSSH), and SDOs oxidize GSSH to sulfite and GSH. However, SDOs have not been characterized for bacteria, including chemolithotrophs. The gene coding for human SDO (human ETHE1 [hETHE1]) in mitochondria was discovered because its mutations lead to a hereditary human disease, ethylmalonic encephalopathy. Using sequence analysis and activity assays, we discovered three subgroups of bacterial SDOs in the proteobacteria and cyanobacteria. Ten selected SDO genes were cloned and expressed in Escherichia coli , and the recombinant proteins were purified. The SDOs used Fe~(2+) for catalysis and displayed considerable variations in specific activities. The wide distribution of SDO genes reveals the likely source of the hETHE1 gene and highlights the potential of sulfur oxidation by heterotrophic bacteria.
机译:溶化营养细菌的硫氧化是众所周知的。但是,通常会忽略异养细菌的硫氧化。硫双加氧酶(SDOs)(EC 1.13.11.18)最初是作为谷胱甘肽(GSH)依赖的硫双加氧酶而存在于某些化学营养型细菌的细胞提取物中的。 GSH自发地与元素硫反应生成谷胱甘肽过硫化物(GSSH),SDO将GSSH氧化成亚硫酸盐和GSH。但是,SDO尚未针对细菌(包括化学营养缺陷型)进行鉴定。人们发现线粒体中编码人类SDO的基因(人类ETHE1 [hETHE1])是因为其突变会导致人类遗传性疾病,即丙二酸脑病。使用序列分析和活性分析,我们发现了变形细菌和蓝细菌中细菌SDO的三个亚组。克隆了十个选定的SDO基因并在大肠杆菌中表达,并纯化了重组蛋白。 SDO使用Fe〜(2+)进行催化,并且比活度表现出很大的变化。 SDO基因的广泛分布揭示了hETHE1基因的可能来源,并突出了异养细菌氧化硫的潜力。

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