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 Lettjournal_title
FEMS microbiology lettersauthors
Kurth JM,Schuster A,Seel W,Herresthal S,Simon J,Dahl Cdoi
10.1093/femsle/fnx003subject
Has Abstractpub_date
2017-02-01 00:00:00issue
3eissn
0378-1097issn
1574-6968pii
fnx003journal_volume
364pub_type
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