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Literature summary extracted from

  • Gao, Y.; Meyer, B.; Sokolova, L.; Zwicker, K.; Karas, M.; Brutschy, B.; Peng, G.; Michel, H.
    Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors (2012), Proc. Natl. Acad. Sci. USA, 109, 3275-3280.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.11 cyanide
-
Aquifex aeolicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.11 membrane
-
Aquifex aeolicus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.11 Cu2+ heme-copper terminal oxidase Aquifex aeolicus
1.10.3.11 Fe2+ heme-copper terminal oxidase Aquifex aeolicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.11 5200
-
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry Aquifex aeolicus
1.10.3.11 16800
-
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry Aquifex aeolicus
1.10.3.11 63900
-
1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry Aquifex aeolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.10.3.11 2 ubiquinol + O2 Aquifex aeolicus
-
2 ubiquinone + 2 H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.11 Aquifex aeolicus G5DGC8 subunit II, Coxb2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.11 native enzyme from membranes by anion exchange chromatography and gel filtration Aquifex aeolicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.11 2 ubiquinol + O2
-
Aquifex aeolicus 2 ubiquinone + 2 H2O
-
?
1.10.3.11 additional information the enzyme is able to oxidize both reduced cytochrome c and ubiquinol Aquifex aeolicus ?
-
?

Subunits

EC Number Subunits Comment Organism
1.10.3.11 More subunit composition and structures, overview. No cytochrome bc1 complex subunit Aquifex aeolicus
1.10.3.11 trimer 1 * 63900, subunit I CoxA2, + 1 * 16800, subunit II CoxB2, + 1 * 5200, subunit IIa, about, mass spectrometry Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
1.10.3.11 Cox2
-
Aquifex aeolicus
1.10.3.11 cytochrome ba3 oxidase
-
Aquifex aeolicus
1.10.3.11 heme-copper terminal oxidase
-
Aquifex aeolicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.10.3.11 heme b
-
Aquifex aeolicus
1.10.3.11 heme c
-
Aquifex aeolicus
1.10.3.11 additional information pyridine hemochromes of extracted hemes Aquifex aeolicus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.10.3.11 Aquifex aeolicus band 1, isoelectric focusing
-
6.4
1.10.3.11 Aquifex aeolicus band 2, isoelectric focusing
-
7

General Information

EC Number General Information Comment Organism
1.10.3.11 evolution the cytochrome ba3 oxidase belongs to the family B of the heme-copper containing terminal oxidases, heme-copper oxidases use either c-type cytochromes or quinols as electron donors Aquifex aeolicus
1.10.3.11 additional information the enzyme can be reduced by ubiquinol, but it alone can also be reduced by decylubiquinol and N,N,N',N'-tetramethyl-4-phenylenediamine/ascorbate in the presence of cyanide Aquifex aeolicus