Tetrathionate | 15536-54-6

• 分子结构分类: 无机化合物 - 均质非金属化合物 - 非金属氧阴离子化合物
• 英文名称: Tetrathionate
• CAS: 15536-54-6
• 化学式: O6S4-2
• 分子量: 224.3
• InChiKey: HPQYKCJIWQFJMS-UHFFFAOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  10
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  182
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  水 、 Tetrathionate 生成 氢(+1)阳离子 、 硫酸酯 、 硫磺 、 dioxido-oxo-sulfanylidene-λ6-sulfane;hydron
  参考文献：
  名称：

  Identification of a gene encoding a tetrathionate hydrolase in Acidithiobacillus ferrooxidans

  摘要：

  Tetrathionate is one of the most important intermediates in dissimilatory sulfur oxidation and can itself be utilized as a sole energy source by some sulfur-oxidizing microorganisms. Tetrathionate hydrolase (4THase) plays a significant role in tetrathionate oxidation and should catalyze the initial step in the oxidative dissimilation when sulfur-oxidizing bacteria are grown on tetrathionate. 4THase activity was detected in tetrathionate-grown Acidithiobacillus ferrooxidans ATCC 23270 cells but not in iron-grown cells. A 4THase having a dimeric structure of identical 50 kDa polypeptides was purified from tetrathionate-grown cells. The 4THase showed the maximum activity at pH 3.0 and high stability under acidic conditions. An open reading frame (ORF) encoding the N-terminal amino acid sequence of the purified 4THase was identified by a BLAST search using the database for the A. ferrooxidans ATCC 23270 genome. Heterologous expression of the gene in Escherichia coli resulted in the formation of inclusion bodies of the protein in an inactive form. Antisera against the recombinant protein clearly recognized the purified native 4THase, indicating that the ORF encoded the 4THase. (C) 2007 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.jbiotec.2007.08.030
• 作为产物：
  描述：

  2,3-二乙氧基-5-甲基-6-癸基-1,4-苯醌 、 dioxido-oxo-sulfanylidene-λ6-sulfane;hydron 生成 decylubiquinol 、 Tetrathionate
  参考文献：
  名称：

  硫氧化途径与双氧还原途径的耦合：新型膜结合硫代硫酸盐：醌氧化还原酶的表征。

  摘要：

  硫代硫酸盐是嗜热古生古细菌Acidianus ambivalens中元素硫氧化途径初始步骤的产物之一。在该生物的需氧生长细胞的膜提取物中发现了一种新的硫代硫酸盐：醌氧化还原酶（TQO）活性。从溶解的膜级分中纯化酶21倍。TQO氧化了硫代硫酸盐，产物为四硫代酸盐，铁氰化物或癸基泛醌（DQ）为电子受体。铁氰化物的最大比活在92摄氏度和pH 6下为73.4 U（mg蛋白质）（-1），DQ在80摄氏度下为397 mU（mg蛋白质）（-1）。Km值为2.6 mM对于硫代硫酸盐（k（cat）= 167 s（-1）），对于铁氰化物为3.4 mM，对于DQ为5.87 micro M. 亚硫酸盐（Ki = 5 micro M），偏亚硫酸氢盐，连二亚硫酸盐和TritonX-100，但不被硫酸盐或四硫代硫酸盐。Caldariella quinone，sulfolobus quinone和menaquinone的

  DOI：

  10.1111/j.1365-2958.2004.04193.x

文献信息

• Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum
  作者：José A. Brito、Kevin Denkmann、Inês A.C. Pereira、Margarida Archer、Christiane Dahl

  DOI：10.1074/jbc.m114.623397

  日期：2015.4

  Although the oxidative condensation of two thiosulfate anions to tetrathionate constitutes a well documented and significant part of the natural sulfur cycle, little is known about the enzymes catalyzing this reaction. In the purple sulfur bacterium Allochromatium vinosum, the reaction is catalyzed by the periplasmic diheme c-type cytochrome thiosulfate dehydrogenase (TsdA). Here, we report the crystal

  尽管两个硫代硫酸根阴离子的氧化缩合成四硫代酸根构成了充分证明的自然硫循环的重要部分，但对催化该反应的酶知之甚少。在紫色硫细菌变色菌Allochromatium v​​inosum中，该反应由周质双血红素c型细胞色素硫代硫酸盐脱氢酶（TsdA）催化。在这里，我们报告了1.98 A分辨率的A. vinosum TsdA的“孤立的形式”的晶体结构和不同分辨率的酶的几种氧化还原状态的晶体结构。该蛋白包含两个典型的I类c型细胞色素结构域，它们围绕由His（53）/ Cys（96）和His（164）/ Lys（208）轴向协调的两个血红素包裹。这些结构域非常相似，表明进化过程中发生了基因复制事件。还原酶后观察到从Lys（208）到Met（209）的配体转换。Cys（96）是催化必不可少的残基，在几个TsdA-Cys（96）变体中，该酶的比活性被完全废除。TsdA-K208N，K208G和M209G变体
• Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase
  作者：Julia M. Kurth、José A. Brito、Jula Reuter、Alexander Flegler、Tobias Koch、Thomas Franke、Eva-Maria Klein、Sam F. Rowe、Julea N. Butt、Kevin Denkmann、Inês A.C. Pereira、Margarida Archer、Christiane Dahl

  DOI：10.1074/jbc.m116.753863

  日期：2016.11

  In the oxidized state, this tetraheme cytochrome c contains three hemes with axial His/Met ligation, while heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Interestingly, thiosulfate is covalently bound to Cys330 on heme 3. In several bacteria including Allochromatium vinosum, TsdB is not present, precluding a general and essential role for electron flow. Both, AvTsdA and the

  硫代硫酸盐脱氢酶（TsdA）家族的酶是广泛使用的二血红素c型细胞色素。在这里，对氧化还原载体进行了研究，该载体介导了硫代硫酸盐氧化产生的电子流进入呼吸或光合电子链。在许多生物中，包括中间型Thiomonas intermedia和Sideroxydans lithotrophicus，tsdA基因紧随tsdB编码另一种双血红素细胞色素。分光光度法结合溶液中的酶促测定表明，当TsdA和TsdB源自同一来源生物时，TsdB在体外可作为TsdA的有效电子受体。TsdA覆盖300 mV至+150 mV的范围，而TsdB在-100至+300 mV之间具有氧化还原活性，因此可以在这些血红蛋白之间进行电子转移。紫色硫磺细菌紫细菌Marichromatium purpuratum的TsdB-TsdA融合蛋白的三维结构通过X射线晶体学解析为2.75 A分辨率，可提供内部电子转移的见解。在氧化状态下，该四血红素细胞色素c包含三个具有轴向His
• Thiosulphate oxidation in the phototrophic sulphur bacterium<i>Allochromatium vinosum</i>
  作者：Daniela Hensen、Detlef Sperling、Hans G. Trüper、Daniel C. Brune、Christiane Dahl

  DOI：10.1111/j.1365-2958.2006.05408.x

  日期：2006.11

  SummaryTwo different pathways for thiosulphate oxidation are present in the purple sulphur bacterium Allochromatium vinosum: oxidation to tetrathionate and complete oxidation to sulphate with obligatory formation of sulphur globules as intermediates. The tetrathionate:sulphate ratio is strongly pH‐dependent with tetrathionate formation being preferred under acidic conditions. Thiosulphate dehydrogenase, a constitutively expressed monomeric 30 kDa c‐type cytochrome with a pH optimum at pH 4.2 catalyses tetrathionate formation. A periplasmic thiosulphate‐oxidizing multienzyme complex (Sox) has been described to be responsible for formation of sulphate from thiosulphate in chemotrophic and phototrophic sulphur oxidizers that do not form sulphur deposits. In the sulphur‐storing A. vinosum we identified five sox genes in two independent loci (soxBXA and soxYZ). For SoxA a thiosulphate‐dependent induction of expression, above a low constitutive level, was observed. Three sox‐encoded proteins were purified: the heterodimeric c‐type cytochrome SoxXA, the monomeric SoxB and the heterodimeric SoxYZ. Gene inactivation and complementation experiments proved these proteins to be indispensable for thiosulphate oxidation to sulphate. The intermediary formation of sulphur globules in A. vinosum appears to be related to the lack of soxCD genes, the products of which are proposed to oxidize SoxY‐bound sulphane sulphur. In their absence the latter is instead transferred to growing sulphur globules.
• Thiosulfate dehydrogenase: a widespread unusual acidophilic<i>c</i>-type cytochrome
  作者：Kevin Denkmann、Fabian Grein、Renate Zigann、Anna Siemen、Johannes Bergmann、Sebastian van Helmont、Anne Nicolai、Inês A. C. Pereira、Christiane Dahl

  DOI：10.1111/j.1462-2920.2012.02820.x

  日期：2012.10

  SummaryIn this work we identified the gene for the tetrathionate‐forming thiosulfate dehydrogenase (TsdA) from the purple sulfur bacterium Allochromatium vinosum by sequence analysis and reverse genetics. The recombinant protein produced in Escherichia coli is a periplasmic, monomeric 25.8 kDa dihaem cytochrome c with an enzyme activity optimum at pH 4. UV‐visible and electron paramagnetic resonance spectroscopy indicate methionine (strictly conserved M222 or M236) and cysteine (C123) as probable sixth distal axial ligands of the two haem irons in TsdA. These results place TsdA in the group of c‐type cytochromes with an unusual axial histidine‐cysteine coordination of the haem iron. These proteins appear to play a pivotal role in sulfur‐based energy metabolism. Exchange of C123 to glycine rendered thiosulfate dehydrogenase inactive, proving the importance of this residue for catalysis.TsdA homologues are present in α‐, β‐, δ‐, γ‐ and ε‐Proteobacteria. Three of these were produced in E. coli and exhibited the expected enzymatic activity. The widespread occurrence of tsdA agrees with reports of tetrathionate formation not only by specialized sulfur oxidizers but also by many chemoorganoheterotrophs that use thiosulfate as a supplemental but not as the sole energy source.
• Tetrathionate stimulated growth of<i>Campylobacter jejuni</i>identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria
  作者：Yang-Wei Liu、Kevin Denkmann、Konrad Kosciow、Christiane Dahl、David J. Kelly

  DOI：10.1111/mmi.12176

  日期：2013.4

  SummaryTetrathionate (S4O62−) is used by some bacteria as an electron acceptor and can be produced in the vertebrate intestinal mucosa from the oxidation of thiosulphate (S2O32−) by reactive oxygen species during inflammation. Surprisingly, growth of the microaerophilic mucosal pathogen Campylobacter jejuni under oxygen‐limited conditions was stimulated by tetrathionate, although it does not possess any known type of tetrathionate reductase. Here, we identify a dihaem cytochrome c (C8j_0815; TsdA) as the enzyme responsible. Kinetic studies with purified recombinant C. jejuni TsdA showed it to be a bifunctional tetrathionate reductase/thiosulphate dehydrogenase with a high affinity for tetrathionate. A tsdA null mutant still slowly reduced, but could not grow on, tetrathionate under oxygen limitation, lacked thiosulphate‐dependent respiration and failed to convert thiosulphate to tetrathionate microaerobically. A TsdA paralogue (C8j_0040), lacking the unusual His–Cys haem ligation of TsdA, had low thiosulphate dehydrogenase and tetrathionate reductase activities. Our data highlight a hitherto unrecognized capacity of C. jejuni to use tetrathionate and thiosulphate in its energy metabolism, which may promote growth in the host. Moreover, as TsdA represents a new class of tetrathionate reductase that is widely distributed among bacteria, we predict that energy conserving tetrathionate respiration is far more common than currently appreciated.