TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA

Abstract 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 sinc...

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Bibliographic Details
Published in:FEMS microbiology letters 2017-02, Vol.364 (3), p.fnx003
Main Authors: Kurth, Julia M., Schuster, Anja, Seel, Waldemar, Herresthal, Stefanie, Simon, Jörg, Dahl, Christiane
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Biocatalysis
Escherichia coli - metabolism
Lipoproteins - isolation & purification
Lipoproteins - metabolism
Oxidation-Reduction
Oxidoreductases - metabolism
Wolinella - chemistry
Wolinella - enzymology
Wolinella - metabolism
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Summary:Abstract 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. TsdC is a unique lipoprotein from Wolinella succinogenes that enhances specific activity of the bifunctional tetrathionate reductase TsdA in this organism.
ISSN:1574-6968
1574-6968
DOI:10.1093/femsle/fnx003