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Influence of haem environment on the catalytic properties of the tetrathionate reductase TsdA from Campylobacter jejuni.

Abstract：

:Bifunctional dihaem cytochrome c thiosulfate dehydrogenases/tetrathionate reductases (TsdA) exhibit different catalytic properties depending on the source organism. In the human food-borne intestinal pathogen Campylobacter jejuni, TsdA functions as a tetrathionate reductase enabling respiration with tetrathionate as an alternative electron acceptor. In the present study, evidence is provided that Cys138 and Met255 serve as the sixth ligands of Haem 1 and Haem 2 respectively, in the oxidized CjTsdA wt protein. Replacement of Cys138 resulted in a virtually inactive enzyme, confirming Haem 1 as the active site haem. Significantly, TsdA variants carrying amino acid exchanges in the vicinity of the electron-transferring Haem 2 (Met255, Asn254 and Lys252) exhibited markedly altered catalytic properties of the enzyme, showing these residues play a key role in the physiological function of TsdA. The growth phenotypes and tetrathionate reductase activities of a series of ΔtsdA/*tsdA complementation strains constructed in the original host C. jejuni 81116, showed that in vivo, the TsdA variants exhibited the same catalytic properties as the pure, recombinantly produced enzymes. However, variants that catalysed tetrathionate reduction more effectively than the wild-type enzyme did not allow better growth.

journal_name

Biosci Rep

journal_title

Bioscience reports

authors

Kurth JM,Butt JN,Kelly DJ,Dahl C

doi

10.1042/BSR20160457

subject

Has Abstract

pub_date

2016-12-09 00:00:00

issue

6

eissn

0144-8463

issn

1573-4935

pii

BSR20160457

journal_volume

36

pub_type

杂志文章

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