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Kurth, Julia M., Butt, Julea N. 
ORCID: https://orcid.org/0000-0002-9624-5226, Kelly, David J. and Dahl, Christiane
(2016)
Influence of haem environment on the catalytic properties of the tetrathionate reductase TsdA from Campylobacter jejuni.
Bioscience Reports, 36 (6).
ISSN 0144-8463
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Abstract
Bifunctional diheme 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. Here, evidence is provided that Cys138 and Met255 serve as the sixth ligands of Heme 1 and Heme 2, respectively, in the oxidized Cj TsdA wt protein. Replacement of Cys138 resulted in a virtually inactive enzyme, confirming Heme 1 as the active site heme. Significantly, TsdA variants carrying amino acid exchanges in the vicinity of the electron-transferring Heme 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 Δ tsdA/*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 catalyzed tetrathionate reduction more effectively than the wild-type enzyme did not allow better growth.
| Item Type: | Article |
|---|---|
| Additional Information: | Date of Acceptance: 18/10/2016 © 2016 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY). |
| Uncontrolled Keywords: | axial heme ligation,reaction directionality,thiosulfate,tetrathionate reductase,cytochrome c |
| Faculty \ School: | Faculty of Science > School of Chemistry Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Energy Materials Laboratory |
| Related URLs: | |
| Depositing User: | Pure Connector |
| Date Deposited: | 03 Nov 2016 16:00 |
| Last Modified: | 21 Oct 2022 07:32 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/61237 |
| DOI: | 10.1042/BSR20160457 |
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