TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA
TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA
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DOI：
10.1093/femsle/fnx003
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发表时间：
2017-01
影响因子：
2.1
通讯作者：
J. Kurth;Anja Schuster;Waldemar Seel;S. Herresthal;J. Simon;C. Dahl
中科院分区：
文献类型：
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作者：
J. Kurth;Anja Schuster;Waldemar Seel;S. Herresthal;J. Simon;C. Dahl
广泛分布的TsdA家族的二血红素细胞色素c是双功能硫代硫酸盐脱氢酶/连四硫酸盐还原酶。在这里，生物化学信息收集TsdA从ε变形杆菌Wolinella succinogenes（WsTsdA）。在W.琥珀酸酯酶是独特的，因为TsdA与在相同转录方向上紧邻tsdA下游编码的前所未有的脂蛋白TsdC密切相关。从大肠杆菌纯化的WsTsdA催化硫代硫酸盐氧化和连四硫酸盐还原。TsdC和WsTsdA在E.在大肠杆菌中，TsdC介导TsdA的膜附着，并确保其完全的催化活性。这种作用在连四硫酸盐还原方向上比在硫代硫酸盐氧化方向上强得多。它的结论是，TsdAC复合物主要作为一个连四硫酸还原酶在体内。
The diheme cytochromes c of the widespread TsdA family are bifunctional thiosulfate dehydrogenase/tetrathionate reductases. Here, biochemical information was collected about TsdA from the Epsilonproteobacterium Wolinella succinogenes (WsTsdA). The situation in W. succinogenes is unique since TsdA is closely associated with the unprecedented lipoprotein TsdC encoded immediately downstream of tsdA in the same direction of transcription. WsTsdA purified from Escherichia coli catalyzed both thiosulfate oxidation and tetrathionate reduction. After co-production of TsdC and WsTsdA in E. coli, TsdC was found to mediate membrane attachment of TsdA and to ensure its full catalytic activity. This effect was much stronger in the tetrathionate-reducing than in the thiosulfate-oxidizing direction. It is concluded that the TsdAC complex predominantly acts as a tetrathionate reductase in vivo.