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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
?
-
2 thiosulfate + ferricyanide

tetrathionate + ferrocyanide
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
artificial electron acceptor
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
2 thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
artificial electron acceptor
-
-
?
2 thiosulfate + ubiquinone

tetrathionate + ubiquinol
-
-
-
-
?
2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
-
-
-
?
tetrathionate + a reduced electron acceptor

2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
bifunctional tetrathionate reductase/thiosulphate dehydrogenase
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
bifunctional tetrathionate reductase/thiosulphate dehydrogenase
-
-
?
tetrathionate + reduced electron acceptor

2 thiosulfate + oxidized electron acceptor
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
for CjTsdA the maximum rate of tetrathionate reduction is approximately twice that of thiosulfate oxidation
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced methyl viologen

2 thiosulfate + oxidized methyl viologen
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + oxidized methyl viologen
-
-
-
-
r
thiosulfate + oxidized acceptor

tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
additional information

?
-
nonenzymatic reduction of ferricyanide is observed with thiosulfate
-
-
?
additional information
?
-
-
no activity with cytochrome c
-
-
?
additional information
?
-
-
tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
-
-
?
additional information
?
-
-
no activity with cytochrome c
-
-
?
additional information
?
-
-
tetrathionate is the product of the TSD-oxidized thiosulfate, and ferricyanide or ubiquinone are the electron acceptors
-
-
?
additional information
?
-
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
-
the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
-
-
-
additional information
?
-
-
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
?
-
-
the TsdAC complex predominantly acts as a tetrathionate reductase in vivo
-
-
-
2 thiosulfate + ubiquinone

tetrathionate + ubiquinol
-
-
-
-
?
2 thiosulfate + ubiquinone
tetrathionate + ubiquinol
-
-
-
-
?
tetrathionate + a reduced electron acceptor

2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + a reduced electron acceptor
2 thiosulfate + an oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor

2 thiosulfate + oxidized electron acceptor
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
r
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
tetrathionate + reduced electron acceptor
2 thiosulfate + oxidized electron acceptor
-
-
-
-
?
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Fe2+
-
in the enzyme bound hemes
MgSO4
-
slightly stimulating, at 200 mM
Na2SO4
150 mM Na-sulfate is required to generate maximum activity, 60% inhibition at 200 mM
sulfite
activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
additional information
-
no stimulation of the enzyme by Na2SO4 at at 100 mM
KCl

-
200 mM, presence of 200 mM NaCl, 86% of the activity in presence of 200 mM NaCl
KCl
-
moderately stimulating, at 200 mM
MgCl2

-
200 mM, presence of 200 mM NaCl, 68% of the activity in presence of 200 mM NaCl
MgCl2
-
moderately stimulating at 200 mM
NaCl

-
activates, best at 200 mM
NaCl
-
maximum activity in presence of 200 mM NaCl
NaCl
-
stimulates, best at 200 mM
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2-heptyl-4-hydroxy-quinoline N-oxide
2-heptyl-4-hydroxyquinoline N-oxide
Na+
-
inhibitory at high concentration above 200 mM; inihibits at high concentrations
Na2SO3
-
70% inhibition at 1 mM
Sodium sulfate
-
100 mM, presence of 200 mM NaCl, 57% residual activity
sodium sulfite
-
0.1 mM, presence of 200 mM NaCl, 45% residual activity
2-heptyl-4-hydroxy-quinoline N-oxide

-
1 microM, presence of 200 mM NaCl, 12% residual activity
2-heptyl-4-hydroxy-quinoline N-oxide
-
strong inhibition
2-heptyl-4-hydroxyquinoline N-oxide

-
88% inhibition at 0.001 mM
2-heptyl-4-hydroxyquinoline N-oxide
-
strong inhibition
N-ethylmaleimide

-
1 mM, presence of 200 mM NaCl, 84% residual activity
N-ethylmaleimide
-
16% inhibition at 1 mM
Na2SO4

150 mM Na-sulfate is required to generate maximum activity, 60% inhibition at 200 mM
Na2SO4
-
54% inhibition at 200 mM
sulfite

activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
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evolution

-
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
-
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
-
physiological function

-
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
-
additional information

the dissimilatory As(V) reductase of strain PSR-1 shows no tetrathionate reductase activity
additional information
-
the tetrathionate reductase of Salmonella enterica strain 1651 shows no dissimilatory As(V) reductase activity
additional information
-
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
-
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
-
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
-
native enzyme 71.4fold from the solubilized membrane fraction by ultracentrifugation, anion exchange chromatography, dialysis, and ultrafiltration
-
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
-
using chromatography on Phenyl-Sepharose column, CM-cellulose column and hydroxylapatite column
-
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