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Literature summary for 7.1.1.9 extracted from

  • Cvetkov, T.L.; Prochaska, L.J.
    Biophysical and biochemical characterization of reconstituted and purified Rhodobacter sphaeroides cytochrome c oxidase in phospholipid vesicles sheds insight into its functional oligomeric structure (2007), Protein Expr. Purif., 56, 189-196.
    View publication on PubMed

Application

Application Comment Organism
additional information the monomeric form of Rhodobacter sphaeroides COX when reconstituted into a phospholipid bilayer is completely functionally active in its ability to perform electron transfer and proton pumping activities of the enzyme Cereibacter sphaeroides

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Cereibacter sphaeroides 5739
-
additional information cytochrome oxidase unilamellar vesicles (COV). Purified COV contains approximately 1 COX molecule per liposome. Purified COV exhibits similar physical properties as unpurified COV Cereibacter sphaeroides
-
-

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
polyhistidine-labeled protein purified on a Ni-NTA column Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 + H+
-
Cereibacter sphaeroides ferricytochrome c + H2O
-
r
reduced cytochrome c + O2 + H+
-
Cereibacter sphaeroides oxidized cytochrome c + H2O
-
?

Subunits

Subunits Comment Organism
monomer
-
Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
COX
-
Cereibacter sphaeroides
cytochrome c oxidase
-
Cereibacter sphaeroides

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
535
-
ferrocytochrome c purified COV Cereibacter sphaeroides
708
-
ferrocytochrome c unpurified COV Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
heme heme aa3 Cereibacter sphaeroides