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Information on EC 1.8.2.5 - thiosulfate reductase (cytochrome) for references in articles please use BRENDA:EC1.8.2.5Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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thiosulfate reductase (cytochrome)
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sulfite + hydrogen sulfide + 2 ferricytochrome c3 = thiosulfate + 2 ferrocytochrome c3
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thiosulfate disproportionation II (cytochrome)
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sulfite,hydrogen sulfide:ferricytochrome-c3 oxidoreductase (thiosulfate-forming)
The enzyme is found in sulfate-reducing bacteria. The source of the electrons is molecular hydrogen, via EC 1.12.2.1, cytochrome-c3 hydrogenase. The organisms utilize the sulfite that is produced for energy generation by EC 1.8.99.5, dissimilatory sulfite reductase.
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MARPU_02550
gene name
TsdA
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brenda
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UniProt
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UniProt
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sulfate-reducing bacteria
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brenda
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thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
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thiosulfate + reduced benzyl viologen
sulfite + hydrogen sulfide + oxidized benzyl viologen
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about 50% of the rate with methyl viologen
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
additional information
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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thiosulfate + reduced methyl viologen
sulfite + hydrogen sulfide + oxidized methyl viologen
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additional information
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with inner- and outer-labeled 35S-thiosulfate, the enzyme reduces only the outer sulfur atom to hydrogen sulfide. No substrates: sulfate, sulfite, tetrathionate, dithionate. No electron donors: reduced nicotinamide adenine dinucleotide, reduced nicotinamide adenine dinucleotide phosphate, reduced glutathione, or cysteine
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additional information
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enzyme catalyzes the stoichiometric production of hydrogen sulfide and sulfite from thiosulfate. The most efficient coupling is obtained with a system containing cytochromes c3. The enzyme exhibits tetrathionate reductase activity. It does not show sulfite reductase activity
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additional information
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the enzyme catalyzes the reductive dismutation of thiosulfate to sulfide and sulfite. The outer sulfur atom of thiosulfate is reduced to sulfide and the inner sulfur atom is released as sulfite
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thiosulfate + 2 ferrocytochrome c3
sulfite + hydrogen sulfide + 2 ferricytochrome c3
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cytochrome c
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presence of a cytochrome that may be an intermediary hydrogen carrier involved in reducing systems for sulfate and other sulfur compounds
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4-chloromercuribenzoate
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0.02 mM, 100% inhibition. Inhibition can be partially or completely reversed by cysteine
4-hydroxymercuribenzoate
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activity can be restored by cysteine
Ag+
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0.01 mM, 90% inhibition
Hg2+
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0.01 mM, 100% inhibition
iodoacetate
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0.5 mM, 70% inhibition
o-Iodosobenzoate
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0.05 mM, 52% inhibition
N-ethylmaleimide
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N-ethylmaleimide
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0.5 mM, 55% inhibition
sulfite
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sulfite
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3 mM, 45% inhibition
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0.5
thiosulfate
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37°C, pH 7.6
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8.8
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8% of maximum activity
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16300
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sedimentation equilibrium centrifugation
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monomer
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1 * 15500, amino acid analysis
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additional information
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presence of two half-cystine residues per mole of enzyme
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three-dimensional structure of the fusion protein with electron-transferring protein TsdB, to 2.75 A resolution. In the oxidized state, the tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Thiosulfate is covalently bound to Cys330 on heme 3
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enzyme loses activtiy upon freezing and thawing
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-20°C, 33% loss of activity within 2 weeks
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-20°C, lyophilized preparation, stable for at least 1 month
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unstable during purification
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W0DW89_MARPU
541
56656
TrEMBL
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Hatchikian, E.
Purification and properties of thiosulfate reductase from Desulfovibrio gigas
Arch. Microbiol.
105
249-256
1975
Desulfovibrio gigas
brenda
Haschke, R.; Campbell, L.
Thiosulfate reductase of Desulfovibrio vulgaris
J. Bacteriol.
106
603-607
1971
Desulfovibrio vulgaris
brenda
Nakatsukasa, W.; Akagi, J.
Thiosulfate reductase isolated from Desulfotomaculum nigrificans
J. Bacteriol.
98
429-433
1969
Desulfotomaculum nigrificans
brenda
Ishimoto, M.; Koyama, J.
Biochemical studies on sulfate-reducing bacteria: VI. separation of hydrogenase and thiosulfate reductase and partial purification of cytochrome and green pigment
J. Biochem.
44
233-242
1957
uncultured bacterium
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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
Marichromatium purpuratum (W0DW89), Marichromatium purpuratum 984 (W0DW89)
brenda
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