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Literature summary for 7.1.1.9 extracted from

  • Arciello, M.; Capo, C.R.; Cozzolino, M.; Ferri, A.; Nencini, M.; Carri, M.T.; Rossi, L.
    Inactivation of cytochrome c oxidase by mutant SOD1s in mouse motoneuronal NSC-34 cells is independent from copper availability but is because of nitric oxide (2010), J. Neurochem., 112, 183-192.
    View publication on PubMed

Application

Application Comment Organism
medicine the copper-enzyme cytochrome c oxidase has been indicated as a primary molecular target of mutant copper, zinc superoxide dismutase in familial amyotrophic lateral sclerosis Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Mus musculus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
copper
-
Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ferrocytochrome c + O2 + H+ Mus musculus
-
ferricytochrome c + H2O
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mitochondria are prepared Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
NSC-34 cell
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 + H+
-
Mus musculus ferricytochrome c + H2O
-
?

Subunits

Subunits Comment Organism
oligomer
-
Mus musculus

Synonyms

Synonyms Comment Organism
complex IV of the mitochondrial electron transport chain
-
Mus musculus
cytochrome c oxidase
-
Mus musculus
CytOX
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
activity assay Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
activity assay Mus musculus

Cofactor

Cofactor Comment Organism Structure
heme a
-
Mus musculus
Heme a3
-
Mus musculus

Expression

Organism Comment Expression
Mus musculus mutated human superoxide dismutase, SOD1, decreases the Cytox activity, but not the protein content of the Cytox subunit II down