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Information on EC 1.8.5.2 - thiosulfate dehydrogenase (quinone) for references in articles please use BRENDA:EC1.8.5.2
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EC Tree
IUBMB Comments The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
thiosulfate:quinone oxidoreductase, thiosulphate:quinone oxidoreductase, tetrathionate-forming thiosulfate dehydrogenase,
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tetrathionate-forming thiosulfate dehydrogenase
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thiosulfate oxidoreductase
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thiosulfate oxidoreductase tetrathionate-forming
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thiosulfate:quinone oxidoreductase
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thiosulphate:quinone oxidoreductase
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2 thiosulfate + 6-decylubiquinone = tetrathionate + 6-decylubiquinol
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thiosulfate:6-decylubiquinone oxidoreductase
The reaction can also proceed with ferricyanide as the electron acceptor, but more slowly. Unlike EC 1.8.2.2, thiosulfate dehydrogenase, this enzyme cannot utilize cytochrome c as an acceptor.
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2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
the physiological electron acceptor is most probably a caldariella quinone type quinone
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tetrathionate + reduced methylene blue
thiosulfate + oxidized methylene blue
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thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
thiosulfate + ferricyanide
tetrathionate + ferrocyanide
thiosulfate + ferricyanide + H+
tetrathionate + ferrocyanide
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when the concentration of thiosulfate is lower than 4 mM, no enzyme activity is detected
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additional information
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thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
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thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
the enzyme couples sulfur compound oxidation with quinone reduction
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thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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thiosulfate + ferricyanide
tetrathionate + ferrocyanide
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r
additional information
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horse heart cytochrome c is not reduced
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additional information
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horse heart cytochrome c is not reduced
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additional information
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the enzyme reduces neither ubiquinone nor horse heart cytochrome c, which serves as an electron acceptor
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2 thiosulfate + caldariellaquinone + 2 H+
tetrathionate + caldariellaquinol
P97224 AND P97207
the physiological electron acceptor is most probably a caldariella quinone type quinone
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r
thiosulfate + 6-decylubiquinone
tetrathionate + 6-decylubiquinol
P97224 AND P97207
the enzyme couples sulfur compound oxidation with quinone reduction
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additional information
a mixture of caldariella quinone, Sulfolobus quinone and menaquinone is non-covalently bound to the protein
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additional information
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does not contain heme
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Dithionite
; 1 mM, complete inhibition
Metabisulfite
; 1 mM, complete inhibition
N-ethylmaleimide
1 mM, 54% inhibition
reduced titanium citrate
1 mM, 65% inhibition
Sodium sulfate
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60% reduction in enzyme activity is observed in the reaction mixture containing 200 mM sodium sulfate
Triton X-100
; 1%, complete inhibition
Zn2+
; 1 mM, 37% inhibition, 5 mM, 82% inhibition
additional information
no inhibition by sulfate or tetrathionate
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sulfite
; 0.005 mM, 48% inhibition, 0.05 mM, complete inhibition
sulfite
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almost complete inhibition in the presence of 10 mM sulfite
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Sodium sulfate
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the purified enzyme requires 150 mM sodium sulfate to generate maximum activity
sulfite
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the addition of sulfite (2 mM) results in the activation of the enzyme at a magnitude of 1.6fold
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0.00587 - 0.0059
6-decylubiquinone
3.4
ferricyanide
; 80°C, pH 6.0
0.00587
6-decylubiquinone
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0.0059
6-decylubiquinone
80°C, pH 6.0
2.6
thiosulfate
; 80°C, pH 6.0
8
thiosulfate
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recombinant enzyme, at pH 2.5 and 50°C
15
thiosulfate
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native enzyme, at pH 2.5 and 70°C
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167
thiosulfate
; 80°C, pH 6.0
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0.005
sulfite
; pH 6.0, 80°C
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0.05
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unpurified recombinant enzyme, at pH 2.5 and 40°C
0.397
activity with decyl ubiquinone at pH 6, 92°C
3.16
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recombinant enzyme after 63.2fold purification, at pH 2.5 and 40°C
49.9
with ferricyanide as electron acceptor
73.4
activity with ferricyanide at pH 6, 92°C
397
with 6-decylubiquinone as electron acceptor
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2.5
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native and recombinant enzyme
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2 - 3
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the native enzyme shows about 35% activity at pH 2.0 and 20% activity at pH 3.0, the recombinant enzyme shows about 80% activity at pH 2.0 and about 35% activity at pH 3.0
3.5 - 6.8
approx. 55% of maximal activity at pH 3.5, approx. 22% of maximal activity at pH 6.5
4.5 - 5.5
pH 4.5: about 70% of maximal activity, pH 5.5: about 35% of maximal activity
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20 - 92
increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons
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20 - 92
increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons
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UnIProt
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DOXA_ACIAM
168
1
18757
Swiss-Prot
DOXD_ACIAM
184
4
20410
Swiss-Prot
A0A1B2GTK3_STRNR
149
4
16751
TrEMBL
A0A1Y0X5I8_BACAM
134
4
14415
TrEMBL
A4YDN8_METS5
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
182
3
20042
TrEMBL
A0A087S200_9ARCH
139
4
14490
TrEMBL
A0A087RRL5_9ARCH
140
3
15212
TrEMBL
F9VNN5_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
168
1
18410
TrEMBL
A0A088E3I8_9CREN
166
1
18421
TrEMBL
A0A1E3L3Y2_9BACL
174
4
19043
TrEMBL
A0A087RYC8_9ARCH
139
4
14490
TrEMBL
A0A2W0CU64_9BACL
179
3
19631
TrEMBL
G0L8D0_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
338
5
37833
TrEMBL
A0A081S6L4_9ARCH
140
3
15212
TrEMBL
A0A088E409_9CREN
182
3
20042
TrEMBL
A0A2W0D2Y3_9BACL
132
4
13566
TrEMBL
A0A288Q5A7_9LACT
174
2
19204
TrEMBL
A0A081RLD8_9ARCH
139
4
14490
TrEMBL
Q96ZH9_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
180
3
19909
TrEMBL
A0A081RPE0_9ARCH
140
3
15212
TrEMBL
A0A087S953_9ARCH
139
4
14490
TrEMBL
A0A081S6J7_9ARCH
139
4
14490
TrEMBL
A0A0B8N5Y9_9NOCA
151
0
15133
TrEMBL
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16000
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
18700
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
20400
alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence
25000
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x * 25000, SDS-PAGE
28000
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
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tetramer
alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE; alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence; alpha2beta2, the 28000 Da subunit and the 16000 Da subunit are identical to to DoxA and DoxD from Acidianus ambivalens quinol:oxygen oxidoreductase, 2 * 16000 + 2 * 28000, SDS-PAGE
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glycoprotein
the larger subunit (28000 Da) appears to be glycosylated
phosphoprotein
glycosylation of subunit DoxA, i.e. beta subunit of TQO
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; solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose
affinity matrix HR 5/5 column chromatography, matrices based on cytochrome c immobilized on crosslinked triazine (2,4,6-tris(aminoethylamine)-1,3,5-triazine), cytochrome c immobilized on Silasorb-amine with carbodiimide activation and cytochrome c immobilized on Sepharose CL-4B
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ammonium sulfate precipitation, CM-650M column chromatography, butyl-650M column chromatography, and TSKgel G3000 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Muller, F.H.; Bandeiras, T.M.; Urich, T.; Teixeira, M.; Gomes, C.M.; Kletzin, A.
Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase
Mol. Microbiol.
53
1147-1160
2004
Acidianus ambivalens, Acidianus ambivalens (P97224 AND P97207)
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, Acidithiobacillus ferrooxidans CCM 4253
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
brenda
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