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 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.

journal_name

FEMS Microbiol Lett

authors

Kurth JM,Schuster A,Seel W,Herresthal S,Simon J,Dahl C

doi

10.1093/femsle/fnx003

subject

Has Abstract

pub_date

2017-02-01 00:00:00

issue

3

eissn

0378-1097

issn

1574-6968

pii

fnx003

journal_volume

364

pub_type

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