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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
additional information
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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
Substrates: -
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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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Substrates: -
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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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Substrates: artificial electron acceptor
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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
Substrates: -
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2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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Substrates: artificial electron acceptor
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2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
Substrates: -
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2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
Substrates: -
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
Substrates: -
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
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Substrates: bifunctional tetrathionate reductase/thiosulphate dehydrogenase
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
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Substrates: -
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
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Substrates: bifunctional tetrathionate reductase/thiosulphate dehydrogenase
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
Substrates: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
Substrates: -
Products: -
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
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Substrates: for CjTsdA the maximum rate of tetrathionate reduction is approximately twice that of thiosulfate oxidation
Products: -
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
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Substrates: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
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Substrates: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
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Substrates: -
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tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
Substrates: -
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tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
Substrates: -
Products: -
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tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
Substrates: -
Products: -
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tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
Substrates: -
Products: -
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
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Substrates: the activity does not couple with mammalian cytochrome c as electron acceptor
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thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
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Substrates: ferricyanide acts as electron acceptor
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thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
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Substrates: the activity does not couple with mammalian cytochrome c as electron acceptor
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thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
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Substrates: ferricyanide acts as electron acceptor
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additional information
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Substrates: nonenzymatic reduction of ferricyanide is observed with thiosulfate
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additional information
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Substrates: no activity with cytochrome c
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additional information
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Substrates: tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
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additional information
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Substrates: no activity with cytochrome c
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additional information
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Substrates: tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
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additional information
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Substrates: the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
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additional information
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Substrates: the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
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additional information
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Substrates: recombinant WsTsdA purified from Escherichia coli catalyzes both thiosulfate oxidation and tetrathionate reduction. Activity measurement by performing thiosulfate-dependent ferricyanide reduction
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2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
additional information
?
-
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Substrates: the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
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2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
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Substrates: -
Products: -
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2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
Substrates: -
Products: -
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
Substrates: -
Products: -
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tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
Substrates: -
Products: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
Substrates: -
Products: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
Substrates: -
Products: -
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
Substrates: -
Products: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
Substrates: -
Products: -
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tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
Substrates: -
Products: -
?
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evolution
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strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
evolution
the enzyme encoded by gene PSR1_00330 belongs to the tetrathionate reductase (TtrA) clade in the DMSO reductase family, phylogenetic analysis. Phylogenetic analysis of gene PSR1_00329 suggested that the encoded TtrB-related proteins does not form a single clade but consists of three distinct clades within the small electron transfer subunits of the DMSO reductase family. The putative psr1_00329-psr1_00330 operon lacked a gene encoding a membrane anchor subunit of tetrathionate reductase (TtrC), but a gene encoding a c-type cytochrome (cyt c) is adjacent to these two genes
evolution
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strain SH might have acquired a unique gene encoding the 44 kDa protein by horizontal transfer, as the protein with a high score and coverage is not found in other Acidithiobacillus thiooxidans genomes
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physiological function
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a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate
physiological function
thiosulfate dehydrogenase plays a significant role in thiosulfate oxidation in the acidophilic, obligately chemolithoautotroph, Acidithiobacillus ferrooxidans
physiological function
-
thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions, cf. EC 1.8.2.2, thiosulfate dehydrogenase. The active site heme 1 in the enzyme has His/Cys ligation in the ferric and ferrous states. In Campylobacter jejuni, TsdA heme 2 has His/Met ligation. Enzyme CjTsdA allows use of tetrathionate as a terminal respiratory electron sink
physiological function
-
a thiosulfate metabolizing enzyme is required for the sulfur-grown cells to metabolize the resulting thiosulfate
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additional information
the dissimilatory As(V) reductase of strain PSR-1 shows no tetrathionate reductase activity
additional information
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the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
additional information
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TsdA is closely associated with the unprecedented lipoprotein TsdC encoded immediately downstream of tsdA in the same direction of transcription. TsdA from Wolinella succinogenes is a periplasmic diheme cytochrome c with hemes, lacking the 21-aa signal peptide. Two Cys-X-X-Cys-His heme c binding motifs are present in the sequence. The active site heme (heme 1) is characterized by an unusual His/Cys axial ligation in TsdA enzymes
additional information
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the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
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71fold enrichment with a recovery of 4.3% of the total activity
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native enzyme 71.4fold from the membrane fraction of strain SH by solubilization with n-dodecyl-beta-D-maltopyranoside, ultracentrifugation, anion exchange chromatography, dialysis, ultrafiltration, and gel filtration
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native enzyme 71.4fold from the solubilized membrane fraction by ultracentrifugation, anion exchange chromatography, dialysis, and ultrafiltration
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native periplasmic enzyme from strain ATCC 23270 and recombinant enzyme from Escherichia coli strain BL21(DE3) celll extract by ammonium sulfate fractionation, cation exchange chromatography, dialysis, hydrophobic interaction chromatography, ultrafilatration, and gel filtration
recombinant Strep-tagged enzyme TsdA 41fold from Escherichia coli strains BL21(DE3) and C43(DE3) by membrane solubilization, affinity chromatography, desalting gel filtration, and ultrafiltration recombinant Strep-tagged TsdC by two steps of ultracentrifugation at 100000 x g, followed by affinity chromatography
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using chromatography on Phenyl-Sepharose column, CM-cellulose column and hydroxylapatite column
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Nakamura, K.; Nakamura, M.; Yoshikawa, H.; Amano, Y.
Purification and properties of thiosulfate dehydrogenase from Acidithiobacillus thiooxidans JCM7814
Biosci. Biotechnol. Biochem.
65
102-108
2001
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans JCM 7814
brenda
Liu, Y.; Denkmann, K.; Kosciow, K.; Dahl, C.; Kelly, D.
Tetrathionate stimulated growth of Campylobacter jejuni identifies a new type of bi-functional tetrathionate reductase (TsdA) that is widely distributed in bacteria
Mol. Microbiol.
88
173-188
2013
Campylobacter jejuni
brenda
Sharmin, S.; Yoshino, E.; Kanao, T.; Kamimura, K.
Characterization of a novel thiosulfate dehydrogenase from a marine acidophilic sulfur-oxidizing bacterium, Acidithiobacillus thiooxidans strain SH
Biosci. Biotechnol. Biochem.
80
273-278
2016
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans SH
brenda
Kikumoto, M.; Nogami, S.; Kanao, T.; Takada, J.; Kamimura, K.
Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans
Appl. Environ. Microbiol.
79
113-120
2013
Acidithiobacillus ferrooxidans (B7J3E3)
brenda
Sharmin, S.; Yoshino, E.; Kanao, T.; Kamimura, K.
Characterization of a novel thiosulfate dehydrogenase from a marine acidophilic sulfur-oxidizing bacterium, Acidithiobacillus thiooxidans strain SH
Biosci. Biotechnol. Biochem.
80
273-278
2016
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans SH
brenda
Muramatsu, F.; Tonomura, M.; Yamada, M.; Kasahara, Y.; Yamamura, S.; Iino, T.; Amachi, S.
Possible involvement of a tetrathionate reductase homolog in dissimilatory arsenate reduction by Anaeromyxobacter sp. strain PSR-1
Appl. Environ. Microbiol.
86
e00829-20
2020
Anaeromyxobacter sp. PSR-1 (A0A0D6QDI4), Salmonella enterica, Salmonella enterica JM1651
brenda
Kurth, J.M.; Schuster, A.; Seel, W.; Herresthal, S.; Simon, J.; Dahl, C.
TsdC, a unique lipoprotein from Wolinella succinogenes that enhances tetrathionate reductase activity of TsdA
FEMS Microbiol. Lett.
364
fnx003
2017
Wolinella succinogenes
brenda
Jenner, L.P.; Kurth, J.M.; van Helmont, S.; Sokol, K.P.; Reisner, E.; Dahl, C.; Bradley, J.M.; Butt, J.N.; Cheesman, M.R.
Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes
J. Biol. Chem.
294
18002-18014
2019
Campylobacter jejuni
brenda