Information on EC 1.8.5.2 - thiosulfate dehydrogenase (quinone)

the physiological electron acceptor is most probably a caldariella quinone type quinone

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r

tetrathionate + reduced methylene blue

thiosulfate + oxidized methylene blue

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-

r

thiosulfate + 6-decylubiquinone

tetrathionate + 6-decylubiquinol

3 entries

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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3 entries

2 thiosulfate + caldariellaquinone + 2 H+

tetrathionate + caldariellaquinol

the physiological electron acceptor is most probably a caldariella quinone type quinone

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r

thiosulfate + 6-decylubiquinone

tetrathionate + 6-decylubiquinol

the enzyme couples sulfur compound oxidation with quinone reduction

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?

additional information

3 entries

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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

sulfite

Triton X-100

1%, complete inhibition

Zn2+

1 mM, 37% inhibition, 5 mM, 82% inhibition

additional information

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Sodium sulfate

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the purified enzyme requires 150 mM sodium sulfate to generate maximum activity

sulfite

-

the addition of sulfite (2 mM) results in the activation of the enzyme at a magnitude of 1.6fold

0.00587 - 0.0059

6-decylubiquinone

3.4

ferricyanide

2.6 - 15

thiosulfate

4 entries

167

thiosulfate

0.005

sulfite

0.05

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unpurified recombinant enzyme, at pH 2.5 and 40Â°C

0.397

activity with decyl ubiquinone at pH 6, 92Â°C

3.16

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recombinant enzyme after 63.2fold purification, at pH 2.5 and 40Â°C

397

with 6-decylubiquinone as electron acceptor

49.9

with ferricyanide as electron acceptor

73.4

activity with ferricyanide at pH 6, 92Â°C

2.5

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native and recombinant enzyme

4.5 - 5

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5

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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

20 - 92

increasing activity is observed in the range between 20 and 92Â°C, a maximum is not observed because of technical reasons

50

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recombinant enzyme

70

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native enzyme

20 - 92

increasing activity is observed in the range between 20 and 92Â°C, a maximum is not observed because of technical reasons

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UnIProt

Acidithiobacillus ferrooxidans CCM 4253

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659545, 724028

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659545

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culture condition:sulfur-grown cell

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culture condition:tetrathionate-grown cell

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102000

gel filtration

16000

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

?

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x * 25000, SDS-PAGE

tetramer

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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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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659545

ammonium sulfate precipitation, CM-650M column chromatography, butyl-650M column chromatography, and TSKgel G3000 gel filtration

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solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose