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2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
tetrathionate + reduced methyl viologen
2 thiosulfate + methyl viologen
tetrathionate + reduced methylviologen
2 thiosulfate + methylviologen
-
-
-
r
thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
thiosulfate + high-potential non-heme iron protein
tetrathionate + reduced high-potential non-heme iron protein
-
-
-
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
additional information
?
-
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
no catalytic activity below 4 mM thiosulfate. Enzyme catalyzes the formation of 1 mol of tetrathionate from 2 mol of thiosulfate
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
r
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
highest activity
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
stoichiometric ratio of conversion is of 1 mole tetrathionate to 2 mol initial thiosulfate. Enzyme can couple thiosulfate oxidation to electron transport to oxygen
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
stoichiometric ratio of conversion is of 1 mole tetrathionate to 2 mol initial thiosulfate. Enzyme can couple thiosulfate oxidation to electron transport to oxygen
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
-
?
2 thiosulfate + 2 ferricyanide
tetrathionate + 2 ferrocyanide
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation. A ligand switch from Lys208 to Met209 is observed upon reduction of the enzyme
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
in Allochromatium vinosum, enzyme TsdA operates in the direction of tetrathionate formation
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
for AvTsdA the maximum rate of oxidative catalysis greatly exceeds that of reductive catalysis, cofactor with a heme c
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
r
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
2 thiosulfate + 2 ferricytochrome c
tetrathionate + 2 ferrocytochrome c
-
-
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + methyl viologen
very low activity
-
-
?
tetrathionate + reduced methyl viologen
2 thiosulfate + methyl viologen
-
highest activity
-
-
?
thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
-
-
?
thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + cytochrome c
tetrathionate + reduced cytochrome c
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
activity assay
-
-
ir
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
-
-
-
-
?
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
-
-
-
-
?
thiosulfate + ferricytochrome c
tetrathionate + ferrocytochrome c
-
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
phenazine methosulfate and phenazine ethosulfate assayed in the presence of dichlorophenolindophenol and Thialhalivibrio versutus cytochrome c550 support low, but significant enzyme activities
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
Wurster's blue can also serve as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a good electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the activity does not couple with mammalian cytochrome c as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme is active only with ferricyanide, not with native or mammalian cytochrome c
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme is active only with ferricyanide, not with native or mammalian cytochrome c
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
-
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
the enzyme rapidly reduces high-potential nonheme iron protein in the presence of thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
horse cytochrome c is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c of yeast and cytochrome c of tuna act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a good electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
A-50: once induced to oxidize thiosulfate, also reduces tetrathionate to thiosulfate in the presence of an electron donor such as lactate, the possibility cannot be excluded, that a separate tetrathionate-reducing enzyme is induced
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
ferricyanide or native cytochrome c act as electron acceptors
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
cytochrome c acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
mammalian cytochrome c acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
heterotrophic bacterium
-
ferricyanide acts as electron acceptor
-
r
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
only native cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c 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
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c 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
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c 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
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome 557 becames reduced when mixed with thiosulfate, enzyme and a trace of cytochrome 553.5, the omission of either the enzyme or cytochrome 553.5 prevents this reduction
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c553.5 acts as electron acceptor
-
ir
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
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
strictly specific for thiosulfate
-
?
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
-
cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome 557 becames reduced when mixed with thiosulfate, enzyme and a trace of cytochrome 553.5, the omission of either the enzyme or cytochrome 553.5 prevents this reduction
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c553.5 acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
ir
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c of yeast is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
horse cytochrome c is a poor electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide or native cytochrome c act as electron acceptors
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide is a much better electron acceptor than cytochrome c
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
mammalian cytochrome c acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + oxidized acceptor
tetrathionate + reduced acceptor
-
ferricyanide acts as electron acceptor
-
?
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
-
-
-
-
?
thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
-
-
-
-
?
additional information
?
-
-
no activity with: pyrrolo-quinoline quinone, methyl- or benzyl viologen, methylthiazol tetrazolium bromide
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with: NADP+, O2
-
-
?
additional information
?
-
no substrates: sulfite, ubiquinone and horse heart cytochrome c
-
-
?
additional information
?
-
-
no substrates: sulfite, ubiquinone and horse heart cytochrome c
-
-
?
additional information
?
-
the enzyme can reduce neither ubiquinone nor horse heart cytochrome c
-
-
-
additional information
?
-
the enzyme can reduce neither ubiquinone nor horse heart cytochrome c
-
-
-
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with FAD
-
-
?
additional information
?
-
-
no activity with: cytochrome c-552, cytochrome c', cytochrome c-553
-
-
?
additional information
?
-
tetrathionate-dependent methylviologen oxidation and thiosulfate-dependent ferricyanide reduction are measured
-
-
?
additional information
?
-
-
tetrathionate-dependent methylviologen oxidation and thiosulfate-dependent ferricyanide reduction are measured
-
-
?
additional information
?
-
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
the enzyme functions as a tetrathionate reductase and a thiosulfate oxidase, respectively
-
-
-
additional information
?
-
-
when coupled with hydrogenase and methyl viologen, the enzyme stoichiometrically reduces thiosulfate to sulfite and sulfide with consumption of hydrogen. No substrates: sulfite or trithionate
-
-
?
additional information
?
-
-
when coupled with hydrogenase and methyl viologen, the enzyme stoichiometrically reduces thiosulfate to sulfite and sulfide with consumption of hydrogen. No substrates: sulfite or trithionate
-
-
?
additional information
?
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
thiosulfate is covalently bound to Cys330 on heme 3 of TsdA. Di-heme cytochrome TsdB itself is not reactive with thiosulfate but accepts electrons from TsdA even when TsdA and TsdB do not originate from the same organism
-
-
?
additional information
?
-
-
no activity with: benzyl viologen, 2,6-dichloroindophenol, 2,6-dichloroindophenol with phenazine methosulfate, 2,6-dichloroindophenol with phenazine ethosulfate, horse heart cytochrome c with phenazine methosulfate, horse heart cytochrome c with phenazine ethosulfate
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with: benzyl viologen, 2,6-dichloroindophenol, 2,6-dichloroindophenol with phenazine methosulfate, 2,6-dichloroindophenol with phenazine ethosulfate, horse heart cytochrome c with phenazine methosulfate, horse heart cytochrome c with phenazine ethosulfate
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
NAD+, methylene blue, 2,6-dichlorophenol indophenol
-
-
?
additional information
?
-
-
no activity with: NADP+, O2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Lu, W.P.; Kelly, D.P.
Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and the 'trithionate hydrolase' from Thiobacillus tepidarius
J. Gen. Microbiol.
134
877-885
1988
Thermithiobacillus tepidarius
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brenda
Kurek, E.J.
Properties of an enzymatic complex active in sulfite and thiosulfate oxidation by Rhodotorula sp.
Arch. Microbiol.
143
277-282
1985
Rhodotorula sp.
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brenda
Then, J.; Truper, H.G.
The role of thiosulfate in sulfur metabolism of Rhodopseudomonas globiformis
Arch. Microbiol.
130
143-146
1981
Rhodopila globiformis
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brenda
Schook, L.B.; Berk, R.S.
Partial purification and characterization of thiosulfate oxidase from Pseudomonas aeruginosa
J. Bacteriol.
140
306-308
1979
Pseudomonas aeruginosa
brenda
Fukumori, Y.; Yamanaka, T.
A high potential nonheme iron protein (HiPIP)-Linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum
Curr. Microbiol.
3
117-120
1979
Allochromatium vinosum
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brenda
Lu, W.P.; Kelly, D.P.
Kinetic and energetic aspects of inorganic sulphur compound oxidation by Thiobacillus tepidarius
J. Gen. Microbiol.
134
865-876
1988
Thermithiobacillus tepidarius
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brenda
Trudinger, P.A.
Metabolism of thiosulfate and tetrathionate by heterotrophic bacteria from soil
J. Bacteriol.
93
550-559
1967
heterotrophic bacterium
brenda
Suzuki, I.
Mechanisms of inorganic oxidation and energy coupling
Annu. Rev. Microbiol.
28
85-101
1974
Acidithiobacillus ferrooxidans, Thiobacillus thioparus
brenda
Trudinger, P.A.
Thiosulfate oxidation and cytochromes in Thiobacillus X
Biochem. J.
78
680-686
1961
Thiobacillus sp., Thiobacillus sp. X
brenda
Tuttle, J.H.; Schwartz, J.H.; Whited, G.M.
Some properties of thiosulfate-oxidizing enzyme from marine heterotroph 16B
Appl. Environ. Microbiol.
46
438-445
1983
Pseudomonas sp.
brenda
Hall, M.R.; Berk, R.S.
Thiosulfate oxidase from an Alcaligenes grown on mercaptosuccinate
Can. J. Microbiol.
18
235-245
1972
Alcaligenes sp.
brenda
Lyric, R.M.; Suzuki, I.
Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. 3. Properties of thiosulfate-oxidizing enzyme and proposed pathway of thiosulfate oxidation
Can. J. Biochem.
48
355-363
1970
Thiobacillus thioparus
brenda
Silver, M.; Lundgren, D.G.
The thiosulfate-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)
Can. J. Biochem.
46
1215-1220
1968
Acidithiobacillus ferrooxidans
brenda
Meulenberg, R.; Pronk, J.T.; Hazeu, W.; van Dijken, J.P.; Frank, J.; Bos, P.; Kuenen, J.G.
Purification and partial characterization of thiosulfate dehydrogenase from Thiobacillus acidophilus
J. Gen. Microbiol.
139
2033-2039
1993
Acidiphilium acidophilum
-
brenda
Kelly, D.P.; Wood, A.P.
Enzymes involved in microbiological oxidation of thiosulfate and polythionates
Methods Enzymol.
243
501-510
1994
Acidiphilium acidophilum, Halothiobacillus neapolitanus, Thermithiobacillus tepidarius
-
brenda
Visser, J.M.; De Jong, G.A.H.; Robertson, L.A.; Kuenen, J.G.
Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophic Thiobacillus sp. W5
Arch. Microbiol.
166
372-378
1996
Thiobacillus sp., Thiobacillus sp. W5
brenda
Janiczek, O.; Pokorna, B.; Zemanova, J.; Mandl, M.
Use of immobilized cytochrome c as a ligand for affinity chromatography of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans
J. Biotechnol.
117
293-298
2005
Acidithiobacillus ferrooxidans
brenda
Sorokin, D.Y.; Tourova, T.P.; Muyzer, G.
Oxidation of thiosulfate to tetrathionate by an haloarchaeon isolated from hypersaline habitat
Extremophiles
9
501-504
2005
halophilic bacterium
brenda
Hensen, D.; Sperling, D.; Trueper, H.G.; Brune, D.C.; Dahl, C.
Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum
Mol. Microbiol.
62
794-810
2006
Allochromatium vinosum
brenda
Janiczek, O.; Zemanova, J.; Mandl, M.
Purification and some properties of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans
Prep. Biochem. Biotechnol.
37
101-111
2007
Acidithiobacillus ferrooxidans
brenda
Dam, B.; Mandal, S.; Ghosh, W.; Das Gupta, S.K.; Roy, P.
The S4-intermediate pathway for the oxidation of thiosulfate by the chemolithoautotroph Tetrathiobacter kashmirensis and inhibition of tetrathionate oxidation by sulfite
Res. Microbiol.
158
330-338
2007
Advenella mimigardefordensis
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), Acidithiobacillus ferrooxidans
brenda
Denkmann, K.; Grein, F.; Zigann, R.; Siemen, A.; Bergmann, J.; van Helmont, S.; Nicolai, A.; Pereira, I.A.; Dahl, C.
Thiosulfate dehydrogenase: a widespread unusual acidophilic c-type cytochrome
Environ. Microbiol.
14
2673-2688
2012
Allochromatium vinosum (D3RVD4), Allochromatium vinosum, Allochromatium vinosum ATCC 17899 (D3RVD4)
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, Campylobacter jejuni NCTC 11828
brenda
Aketagawa, J.; Kobayashi, K.; Ishimoto, M.
Purification and properties of thiosulfate reductase from Desulfovibrio vulgaris, Miyazaki F
J. Biochem.
97
1025-1032
1985
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F
brenda
Kurth, J.M.; Brito, J.A.; Reuter, J.; Flegler, A.; Koch, T.; Franke, T.; Klein, E.M.; Rowe, S.F.; Butt, J.N.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase
J. Biol. Chem.
291
24804-24818
2016
Allochromatium vinosum (D3RVD4), Allochromatium vinosum
brenda
Brito, J.; Gutierres, A.; Denkmann, K.; Dahl, C.; Archer, M.
Production, crystallization and preliminary crystallographic analysis of Allochromatium vinosum thiosulfate dehydrogenase TsdA, an unusual acidophilic c-type cytochrome
Acta Crystallogr. Sect. F
70
1424-1427
2014
Allochromatium vinosum (D3RVD4), Allochromatium vinosum, Allochromatium vinosum ATCC 17899 (D3RVD4)
brenda
Brito, J.A.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum structural and functional insights into thiosulfate oxidation
J. Biol. Chem.
290
9222-9238
2015
Allochromatium vinosum (D3RVD4), Allochromatium vinosum
brenda
Kurth, J.M.; Brito, J.A.; Reuter, J.; Flegler, A.; Koch, T.; Franke, T.; Klein, E.M.; Rowe, S.F.; Butt, J.N.; Denkmann, K.; Pereira, I.A.; Archer, M.; Dahl, C.
Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase
J. Biol. Chem.
291
24804-24818
2016
Allochromatium vinosum (D3RVD4), Allochromatium vinosum, Marichromatium purpuratum (W0DW89), Marichromatium purpuratum, Allochromatium vinosum DSM 180 (D3RVD4), Marichromatium purpuratum 984 (W0DW89)
brenda
Narayan, K.; Sabat, S.; Das, S.
Mechanism of electron transport during thiosulfate oxidation in an obligately mixotrophic bacterium Thiomonas bhubaneswarensis strain S10 (DSM 18181T)
Appl. Microbiol. Biotechnol.
101
1239-1252
2017
Thiomonas bhubaneswarensis, Thiomonas bhubaneswarensis S10
brenda
Wang, R.; Lin, J.; Liu, X.; Pang, X.; Zhang, C.; Yang, C.; Gao, X.; Lin, C.; Li, Y.; Li, Y.; Lin, J.; Chen, L.
Sulfur oxidation in the acidophilic autotrophic Acidithiobacillus spp.
Front. Microbiol.
9
3290
2019
Acidithiobacillus ferrooxidans (B7J3E3), Acidithiobacillus ferrooxidans DSM 14882 (B7J3E3)
brenda
Zhang, J.; Liu, R.; Xi, S.; Cai, R.; Zhang, X.; Sun, C.
A novel bacterial thiosulfate oxidation pathway provides a new clue about the formation of zero-valent sulfur in deep sea
ISME J.
14
2261-2274
2020
Qipengyuania flava, Qipengyuania flava 21-3
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
Allochromatium vinosum, Allochromatium vinosum (D3RVD4), Campylobacter jejuni, Allochromatium vinosum DSM 180 (D3RVD4), Allochromatium vinosum NCIMB 10441 (D3RVD4), Allochromatium vinosum ATCC 17899 (D3RVD4), Allochromatium vinosum NBRC 103801 (D3RVD4), Allochromatium vinosum D (D3RVD4)
brenda
Rameez, M.; Pyne, P.; Mandal, S.; Chatterjee, S.; Alam, M.; Bhattacharya, S.; Mondal, N.; Sarkar, J.; Ghosh, W.
Two pathways for thiosulfate oxidation in the alphaproteobacterial chemolithotroph Paracoccus thiocyanatus SST
Microbiol. Res.
230
126345
2020
Paracoccus thiocyanatus (A0A3D8PFU9), Paracoccus thiocyanatus, Paracoccus thiocyanatus SST (A0A3D8PFU9)
brenda