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本文引用的文献

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Biological and abiological sulfur reduction at high temperatures.高温下的生物和非生物硫还原。
Appl Environ Microbiol. 1985 May;49(5):1057-61. doi: 10.1128/aem.49.5.1057-1061.1985.
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Surface-active substances produced by Thiobacillus thiooxidans.由氧化硫硫杆菌产生的表面活性物质。
J Bacteriol. 1961 Nov;82(5):788-9. doi: 10.1128/jb.82.5.788-789.1961.
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Oxidation of elemental sulfur by an enzyme system of Thiobacillus thiooxidans.氧化硫硫杆菌的酶系统对元素硫的氧化作用。
Biochim Biophys Acta. 1965 Jul 8;104(2):359-71. doi: 10.1016/0304-4165(65)90341-7.
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Scanning electron microscopy of thiobacilli grown on colloïdal sulfur.在胶体硫上生长的硫杆菌的扫描电子显微镜观察。
Arch Microbiol. 1974;99(4):323-9. doi: 10.1007/BF00696246.
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Physiology of the thiobacilli: elucidating the sulphur oxidation pathway.硫杆菌的生理学:阐明硫氧化途径。
Microbiol Sci. 1985;2(4):105-9.
6
A novel and remarkably thermostable ferredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus.一种来自嗜热古细菌激烈火球菌的新型且极其耐热的铁氧化还原蛋白。
J Bacteriol. 1989 Jun;171(6):3433-9. doi: 10.1128/jb.171.6.3433-3439.1989.
7
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.嗜热古细菌激烈火球菌氢化酶的特性研究
J Biol Chem. 1989 Mar 25;264(9):5070-9.
8
Use of nuclepore filters for counting bacteria by fluorescence microscopy.使用核孔滤膜通过荧光显微镜对细菌进行计数。
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多硫化物在嗜热古菌 Pyrococcus furiosus 还原元素硫中的作用。

Role of Polysulfides in Reduction of Elemental Sulfur by the Hyperthermophilic Archaebacterium Pyrococcus furiosus.

机构信息

Department of Chemical Engineering, The Johns Hopkins University, Baltimore, Maryland 21218, and Polymers Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899.

出版信息

Appl Environ Microbiol. 1990 May;56(5):1255-62. doi: 10.1128/aem.56.5.1255-1262.1990.

DOI:10.1128/aem.56.5.1255-1262.1990
PMID:16348181
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC184392/
Abstract

Polysulfides formed through the breakdown of elemental sulfur or other sulfur compounds were found to be reduced to H(2)S by the hyperthermophilic archaebacterium Pyrococcus furiosus during growth. Metabolism of polysulfides by the organism was dissimilatory, as no incorporation of S-labeled elemental sulfur was detected. However, [S]cysteine and [S]methionine were incorporated into cellular protein. Contact between the organism and elemental sulfur is not necessary for metabolism. The sulfide generated from metabolic reduction of polysulfides dissociates to a strong nucleophile, HS, which in turn opens up the S(8) elemental sulfur ring. In addition to H(2)S, P. furiosus cultures produced methyl mercaptan in a growth-associated fashion.

摘要

通过高温古菌 Pyrococcus furiosus 的生长,发现通过元素硫或其他硫化合物的分解形成的多硫化物被还原为 H(2)S。该生物体对多硫化物的代谢是异化的,因为没有检测到 S 标记的元素硫的掺入。然而,[S]半胱氨酸和[S]蛋氨酸被掺入到细胞蛋白中。生物体与元素硫之间的接触不是代谢所必需的。多硫化物代谢还原产生的硫化物离解为强亲核试剂 HS,HS 继而打开 S(8)元素硫环。除了 H(2)S,P. furiosus 培养物以生长相关的方式产生甲硫醇。