The genetic basis of tetrathionate respiration in Salmonella typhimurium
@article{Hensel1999TheGB,
title={The genetic basis of tetrathionate respiration in Salmonella typhimurium},
author={Michael T. Hensel and Andrew P. Hinsley and Thomas Nickelsen Nikolaus and Gary Sawers and Ben C. Berks},
journal={Molecular Microbiology},
year={1999},
volume={32}
}A range of bacteria are able to use tetrathionate as a terminal respiratory electron acceptor. Here we report the identification and characterization of the ttrRSBCA locus required for tetrathionate respiration in Salmonella typhimurium LT2a. The ttr genes are located within Salmonella pathogenicity island 2 at centisome 30.5. ttrA, ttrB and ttrC are the tetrathionate reductase structural genes. Sequence analysis suggests that TtrA contains a molybdopterin guanine dinucleotide cofactor and a…
225 Citations
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References
SHOWING 1-10 OF 102 REFERENCES
A novel Sec‐independent periplasmic protein translocation pathway in Escherichia coli
- BiologyThe EMBO journal
- 1998
The results strongly suggest that the translocation of the molybdoenzyme TMAO reductase into the periplasm uses a mechanism fundamentally different from general protein translocation.
Characterization of the paramagnetic iron‐containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase
- Biology, ChemistryFEBS letters
- 1994
Bacterial Reduction of Tetrathionate
- Biology, ChemistryNature
- 1942
In the course of attempts to improve selective media for isolating Salmonellas and Bact from excreta, it is found that, so far as some organisms are concerned, the tetrathionate is firstreduced to thiosulphate.
Anaerobic respiration with elemental sulfur and with disulfides
- Chemistry, Biology
- 1998
Anaerobic respiration with elemental sulfur/polysulfide or organic disulfides is performed by several bacteria and archaea, but has only been investigated in a few organisms in detail. The electron…
A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins
- BiologyCell
- 1998
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
- ChemistryBiochemistry
- 1998
It is proposed that the transfer of Hf+ from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2.
Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulphide reductase.
- BiologyEuropean journal of biochemistry
- 1992
The polysulphide reductase of Wolinella succinogenes is a component of the phosphorylative electron transport system with polysULphide as the terminal acceptor using an antiserum raised against the major subunit (PsrA, 85 kDa) of the enzyme.
The phs gene and hydrogen sulfide production by Salmonella typhimurium
- BiologyJournal of bacteriology
- 1987
Salmonella typhimurium produces H2S from thiosulfate or sulfite. The respective pathways for the two reductions must be distinct as mutants carrying motations in phs, chlA, and menB reduced sulfite,…
Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters.
- Chemistry, BiologyBiochemistry
- 1996
A proposed model for the coordination of the four Fe-S centers by the four Cys groups of the beta subunit of nitrate reductase A is proposed, in good agreement with the magnitude of intercenter magnetic interactions observed by EPR and with the stability of the different mutants.
Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci
- BiologyJournal of bacteriology
- 1982
The properties of mutants of E. coli which are defective with respect to nitrate reductase activity were examined and it was concluded that the chlE and chlG loci are involved in the synthesis of insertion of molybdenum cofactor.