Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.10.3.11 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
Search for more literature for 1.10.3.11

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
azide
-
 Gluconobacter oxydans
additional information CIO activity is much more resistant to cyanide, compared with Escherichia coli cytochrome bd, but sensitive to azide Gluconobacter oxydans
ubiquinol-1 substrate inhibition Gluconobacter oxydans
ubiquinol-2 substrate inhibition Gluconobacter oxydans
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
ubiquinone-2 product inhibition Gluconobacter oxydans

KM Value [mM]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ubiquinol-1 + O2 Gluconobacter oxydans
-
 2 ubiquinone-1 + 2 H2O
-
 ?
2 ubiquinol-1 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-1 + 2 H2O
-
 ?
2 ubiquinol-10 + O2 Gluconobacter oxydans
-
 2 ubiquinone-10 + 2 H2O
-
 ?
2 ubiquinol-10 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-10 + 2 H2O
-
 ?
2 ubiquinol-2 + O2 Gluconobacter oxydans
-
 2 ubiquinone-2 + 2 H2O
-
 ?
2 ubiquinol-2 + O2 Gluconobacter oxydans NBRC 3172
-
 2 ubiquinone-2 + 2 H2O
-
 ?

Organism

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

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6
-
 Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
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

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

General Information

General Information Comment Organism
evolution the enzyme is a member of the subfamily of cytochrome bd present in bacterial respiratory chain, phylogenetic analysis Gluconobacter oxydans
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
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