Elemental sulfur reduction in the deep-sea vent thermophile, Thermovibrio ammonificans.
Elemental sulfur reduction in the deep-sea vent thermophile, Thermovibrio ammonificans.
复制标题
深海喷口嗜热菌、氨化热弧菌中元素硫的还原。
DOI：
10.1111/1462-2920.14280
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发表时间：
2018
影响因子：
5.1
通讯作者：
Vetriani,Costantino
中科院分区：
文献类型：
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作者：
Jelen,Benjamin;Giovannelli,Donato;Falkowski,PaulG;Vetriani,Costantino
单质硫的还原是地热环境中原核生物重要的节能途径，在地热环境中，硫呼吸有助于硫的生物地球化学循环。尽管如此，在大多数微生物中，单质硫还原为硫化氢的途径仍不清楚。我们利用深海热流菌thermovibrio amonificans（一种深海热流菌，通过氢的氧化和硝酸盐和单质硫的还原来保存能量），结合转录组学和蛋白质组学方法，结合扫描电子显微镜进行了综合生长实验。我们的研究结果显示，FAD依赖性吡啶核苷酸二硫还原酶家族的两个成员，分别类似于硫醌还原酶和NADH依赖性硫还原酶（NSR），在硫呼吸过程中过度表达。扫描电子显微图和固硫实验表明，可直接获取ofT。氨和硫颗粒强烈促进生长。硫的代谢。氨化反应似乎需要在酸性pH下从块状单质硫到多硫化物再到纳米粒硫的非生物转变，再加上生物氢氧化。提出了一种由NSR样蛋白作为末端还原酶介导的生物-非生物硫呼吸耦合机制。
The reduction of elemental sulfur is an important energy‐conserving pathway in prokaryotes inhabiting geothermal environments, where sulfur respiration contributes to sulfur biogeochemical cycling. Despite this, the pathways through which elemental sulfur is reduced to hydrogen sulfide remain unclear in most microorganisms. We integrated growth experiments usingThermovibrio ammonificans, a deep‐sea vent thermophile that conserves energy from the oxidation of hydrogen and reduction of both nitrate and elemental sulfur, with comparative transcriptomic and proteomic approaches, coupled with scanning electron microscopy. Our results revealed that two members of the FAD‐dependent pyridine nucleotide disulfide reductase family, similar to sulfide‐quinone reductase and to NADH‐dependent sulfur reductase (NSR), respectively, are over‐expressed during sulfur respiration. Scanning electron micrographs and sulfur sequestration experiments indicated that direct access ofT. ammonificansto sulfur particles strongly promoted growth. The sulfur metabolism ofT. ammonificansappears to require abiotic transition from bulk elemental sulfur to polysulfide to nanoparticulate sulfur at an acidic pH, coupled to biological hydrogen oxidation. A coupled biotic‐abiotic mechanism for sulfur respiration is put forward, mediated by an NSR‐like protein as the terminal reductase.