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Literature summary extracted from

  • Miura, H.; Mogi, T.; Ano, Y.; Migita, C.T.; Matsutani, M.; Yakushi, T.; Kita, K.; Matsushita, K.
    Cyanide-insensitive quinol oxidase (CIO) from Gluconobacter oxydans is a unique terminal oxidase subfamily of cytochrome bd (2013), J. Biochem., 153, 535-545.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.3.11 genes cioA and cioB encoding subunits I and II, phylogenetic analysis Gluconobacter oxydans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.11 azide
-
 Gluconobacter oxydans
1.10.3.11 additional information CIO activity is much more resistant to cyanide, compared with Escherichia coli cytochrome bd, but sensitive to azide Gluconobacter oxydans
1.10.3.11 ubiquinol-1 substrate inhibition Gluconobacter oxydans
1.10.3.11 ubiquinol-2 substrate inhibition Gluconobacter oxydans
1.10.3.11 ubiquinone-1 product inhibition, an excess amount of ubiquinol-2 is unable to suppress product inhibition with ubiquinone-1 therefore, the inhibition mode may not be competitive Gluconobacter oxydans
1.10.3.11 ubiquinone-2 product inhibition Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.11 additional information
-
 additional information Michaelis-Menten kinetics, overview Gluconobacter oxydans
1.10.3.11 0.0729
-
 ubiquinol-1 pH 6.5, 35°C Gluconobacter oxydans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.11 membrane outer surface of the cytoplasmic membrane Gluconobacter oxydans 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.11 Fe2+ heme iron, 3.1 Fe2+ per enzyme molecule Gluconobacter oxydans
1.10.3.11 additional information the enzyme contains no copper Gluconobacter oxydans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.11 30000
-
 x * 53000 + x * 30000, SDS-PAGE Gluconobacter oxydans
1.10.3.11 53000
-
 x * 53000 + x * 30000, SDS-PAGE Gluconobacter oxydans

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-1 + O2 Gluconobacter oxydans
-
 2 ubiquinone-1 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-1 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-1 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-10 + O2 Gluconobacter oxydans
-
 2 ubiquinone-10 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-10 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-10 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-2 + O2 Gluconobacter oxydans
-
 2 ubiquinone-2 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-2 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-2 + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.11 Gluconobacter oxydans
-
 subunit I, CioA; genes cioA and cioB encoding subunits I and II
-
1.10.3.11 Gluconobacter oxydans NBRC 3172
-
 subunit I, CioA; genes cioA and cioB encoding subunits I and II
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.11 native enzyme from membranes by detergent solubilization, anion exchange and hydroxyapatite chromatography Gluconobacter oxydans

Reaction

EC Number Reaction Comment Organism Reaction ID
1.10.3.11 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O modified ping-pong bi-bi mechanism Gluconobacter oxydans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.11 2 ubiquinol-1 + O2
-
 Gluconobacter oxydans 2 ubiquinone-1 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-1 + O2
-
 Gluconobacter oxydans NBRC 3172 2 ubiquinone-1 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-10 + O2
-
 Gluconobacter oxydans 2 ubiquinone-10 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-10 + O2
-
 Gluconobacter oxydans NBRC 3172 2 ubiquinone-10 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-2 + O2
-
 Gluconobacter oxydans 2 ubiquinone-2 + 2 H2O
-
 ?
1.10.3.11 2 ubiquinol-2 + O2
-
 Gluconobacter oxydans NBRC 3172 2 ubiquinone-2 + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.10.3.11 ? x * 53000 + x * 30000, SDS-PAGE Gluconobacter oxydans

Synonyms

EC Number Synonyms Comment Organism
1.10.3.11 CIO
-
 Gluconobacter oxydans
1.10.3.11 cyanide-insensitive quinol oxidase
-
 Gluconobacter oxydans
1.10.3.11 cyanide-insensitive terminal quinol oxidase
-
 Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.11 25
-
 assay at Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.11 5 6
-
 Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.10.3.11 heme the enzyme contains reduced hemes b and of oxygenated and ferric heme d, differing from cytochrome bd. Heme d serves as the ligand-binding site of CIO Gluconobacter oxydans

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.10.3.11 0.82
-
 pH 6.5, 25°C Gluconobacter oxydans azide

General Information

EC Number General Information Comment Organism
1.10.3.11 evolution the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis Gluconobacter oxydans
1.10.3.11 additional information the purified CIO shows an extraordinary high ubiquinol-1 oxidase activity. The enzyme shows a modified ping-pong bi-bi mechanism Gluconobacter oxydans
1.10.3.11 physiological function ubiquinol-10 molecules are reoxidized by cytochrome bo3 and CIO, terminal oxidases of the respiratory chain. In the Gluconobacter oxydans respiratory chain, CIO may have a physiological role in compensation for lower activity of cytochrome bo3 under low growth pH to maintain rapid substrate oxidation Gluconobacter oxydans