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Literature summary extracted from

  • 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 (2004), Mol. Microbiol., 53, 1147-1160.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.5.2 Dithionite 1 mM, complete inhibition Acidianus ambivalens
1.8.5.2 Metabisulfite 1 mM, complete inhibition Acidianus ambivalens
1.8.5.2 additional information no inhibition by sulfate or tetrathionate Acidianus ambivalens
1.8.5.2 N-ethylmaleimide 1 mM, 54% inhibition Acidianus ambivalens
1.8.5.2 reduced titanium citrate 1 mM, 65% inhibition Acidianus ambivalens
1.8.5.2 sulfite 0.005 mM, 48% inhibition, 0.05 mM, complete inhibition Acidianus ambivalens
1.8.5.2 Triton X-100 1%, complete inhibition Acidianus ambivalens
1.8.5.2 Zn2+ 1 mM, 37% inhibition, 5 mM, 82% inhibition Acidianus ambivalens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.5.2 0.00587
-
 6-decylubiquinone
-
 Acidianus ambivalens
1.8.5.2 0.0059
-
 6-decylubiquinone 80°C, pH 6.0 Acidianus ambivalens
1.8.5.2 2.6
-
 thiosulfate
-
 Acidianus ambivalens
1.8.5.2 2.6
-
 thiosulfate 80°C, pH 6.0 Acidianus ambivalens
1.8.5.2 3.4
-
 ferricyanide
-
 Acidianus ambivalens
1.8.5.2 3.4
-
 ferricyanide 80°C, pH 6.0 Acidianus ambivalens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.5.2 membrane
-
 Acidianus ambivalens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.5.2 16000
-
 alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE Acidianus ambivalens
1.8.5.2 16000
-
 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 Acidianus ambivalens
1.8.5.2 18700
-
 alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence Acidianus ambivalens
1.8.5.2 20400
-
 alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence Acidianus ambivalens
1.8.5.2 28000
-
 alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE Acidianus ambivalens
1.8.5.2 28000
-
 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 Acidianus ambivalens
1.8.5.2 102000
-
 gel filtration Acidianus ambivalens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.5.2 2 thiosulfate + caldariellaquinone + 2 H+ Acidianus ambivalens the physiological electron acceptor is most probably a caldariella quinone type quinone tetrathionate + caldariellaquinol
-
 r
1.8.5.2 thiosulfate + 6-decylubiquinone Acidianus ambivalens the enzyme couples sulfur compound oxidation with quinone reduction tetrathionate + 6-decylubiquinol
-
 ?
7.1.1.4 caldariella quinol + O2 + n H+/in Acidianus ambivalens
-
 caldariella quinone + H2O + n H+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.2 Acidianus ambivalens P97224 AND P97207
-
-
7.1.1.4 Acidianus ambivalens P94117 and P94118 P94117 (doxB, catalytic core), P94118 (doxC)
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.8.5.2 glycoprotein the larger subunit (28000 Da) appears to be glycosylated Acidianus ambivalens
1.8.5.2 phosphoprotein glycosylation of subunit DoxA, i.e. beta subunit of TQO Acidianus ambivalens

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.5.2
-
 Acidianus ambivalens
1.8.5.2 solubilization, Q-Sepharose, hydroxylapatite, DEAE-Sepharose Acidianus ambivalens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.5.2 0.397
-
 activity with decyl ubiquinone at pH 6, 92°C Acidianus ambivalens
1.8.5.2 49.9
-
 with ferricyanide as electron acceptor Acidianus ambivalens
1.8.5.2 73.4
-
 activity with ferricyanide at pH 6, 92°C Acidianus ambivalens
1.8.5.2 397
-
 with 6-decylubiquinone as electron acceptor Acidianus ambivalens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.5.2 2 thiosulfate + caldariellaquinone + 2 H+ the physiological electron acceptor is most probably a caldariella quinone type quinone Acidianus ambivalens tetrathionate + caldariellaquinol
-
 r
1.8.5.2 additional information horse heart cytochrome c is not reduced Acidianus ambivalens ?
-
 ?
1.8.5.2 tetrathionate + reduced methylene blue
-
 Acidianus ambivalens thiosulfate + oxidized methylene blue
-
 r
1.8.5.2 thiosulfate + 6-decylubiquinone
-
 Acidianus ambivalens tetrathionate + 6-decylubiquinol
-
 ?
1.8.5.2 thiosulfate + 6-decylubiquinone
-
 Acidianus ambivalens tetrathionate + 6-decylubiquinol
-
 r
1.8.5.2 thiosulfate + 6-decylubiquinone the enzyme couples sulfur compound oxidation with quinone reduction Acidianus ambivalens tetrathionate + 6-decylubiquinol
-
 ?
1.8.5.2 thiosulfate + ferricyanide
-
 Acidianus ambivalens tetrathionate + ferrocyanide
-
 ?
1.8.5.2 thiosulfate + ferricyanide
-
 Acidianus ambivalens tetrathionate + ferrocyanide
-
 r
7.1.1.4 caldariella quinol + O2 + n H+/in
-
 Acidianus ambivalens caldariella quinone + H2O + n H+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.5.2 tetramer alpha2,beta2, 2 * 16000 + 2 * 28000, SDS-PAGE Acidianus ambivalens
1.8.5.2 tetramer alpha2,beta2, 2 * 20400 + 2 * 18700, deduced from nucleotide sequence Acidianus ambivalens
1.8.5.2 tetramer 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 Acidianus ambivalens
7.1.1.4 ? the doxD and doxA genes form a bicistronic operon in the Acidianus ambivalens genome, physically separated from the doxBCEF operon encoding the catalytic and the other subunits of the terminal quinol:oxygen oxidoreductase. Subunits with apparent molecular masses of 56000 Da (DoxB) and 61000 Da (DoxC) appear in the preparation of the terminal oxidase. Both enzymes 1. thiosulfate dehydrogenase (quinone) (EC 1.8.5.2, composed of the subunits DoxA and DoxD) and 2. caldariella quinol:dioxygen oxidoreductase (composed of the major subunits DoxB and DoxC and the minor subunit DoxE) form separate entities. The thiosulfate dehydrogenase (quinone) and the terminal oxidase might still form a loose aggregation in the membrane, transferring electrons rapidly either directly via the bound caldariella quinol molecule or indirectly via free caldariella quinol Acidianus ambivalens

Synonyms

EC Number Synonyms Comment Organism
1.8.5.2 thiosulfate oxidoreductase
-
 Acidianus ambivalens
1.8.5.2 thiosulfate oxidoreductase tetrathionate-forming
-
 Acidianus ambivalens
1.8.5.2 thiosulfate:quinone oxidoreductase
-
 Acidianus ambivalens
1.8.5.2 thiosulphate:quinone oxidoreductase
-
 Acidianus ambivalens
1.8.5.2 TQO
-
 Acidianus ambivalens
7.1.1.4 caldariella quinol:dioxygen oxidoreductase
-
 Acidianus ambivalens
7.1.1.4 cytochrome aa3
-
 Acidianus ambivalens
7.1.1.4 terminal quinol:oxygen oxidoreductase
-
 Acidianus ambivalens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.5.2 20 92 increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons Acidianus ambivalens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.8.5.2 20 92 increasing activity is observed in the range between 20 and 92°C, a maximum is not observed because of technical reasons Acidianus ambivalens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.5.2 167
-
 thiosulfate
-
 Acidianus ambivalens
1.8.5.2 167
-
 thiosulfate 80°C, pH 6.0 Acidianus ambivalens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.5.2 4.5 5
-
 Acidianus ambivalens
1.8.5.2 5
-
-
 Acidianus ambivalens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.8.5.2 3.5 6.8 approx. 55% of maximal activity at pH 3.5, approx. 22% of maximal activity at pH 6.5 Acidianus ambivalens
1.8.5.2 4.5 5.5 pH 4.5: about 70% of maximal activity, pH 5.5: about 35% of maximal activity Acidianus ambivalens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.5.2 additional information a mixture of caldariella quinone, Sulfolobus quinone and menaquinone is non-covalently bound to the protein Acidianus ambivalens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8.5.2 0.005
-
 sulfite
-
 Acidianus ambivalens
1.8.5.2 0.005
-
 sulfite pH 6.0, 80°C Acidianus ambivalens