Kurth, Julia M. ; Schuster, Anja ; Seel, Waldemar ; Herresthal, Stefanie ; Simon, Jörg ; Dahl, Christiane (2017)
TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA.
In: FEMS microbiology letters, 364 (3)
Artikel, Bibliographie
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2017 |
| Autor(en): | Kurth, Julia M. ; Schuster, Anja ; Seel, Waldemar ; Herresthal, Stefanie ; Simon, Jörg ; Dahl, Christiane |
| Art des Eintrags: | Bibliographie |
| Titel: | TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA. |
| Sprache: | Englisch |
| Publikationsjahr: | 2017 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | FEMS microbiology letters |
| Jahrgang/Volume einer Zeitschrift: | 364 |
| (Heft-)Nummer: | 3 |
| Kurzbeschreibung (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. |
| ID-Nummer: | pmid:28062520 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology |
| Hinterlegungsdatum: | 10 Jan 2017 10:57 |
| Letzte Änderung: | 11 Apr 2017 10:10 |
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