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Literature summary for 7.1.1.9 extracted from

  • Liu, J.G.; Naruta, Y.; Tani, F.
    Synthetic models of the active site of cytochrome C oxidase: influence of tridentate or tetradentate copper chelates bearing a His--Tyr linkage mimic on dioxygen adduct formation by heme/Cu complexes (2007), Chemistry, 13, 6365-6378.
    View publication on PubMed
Search for more literature for 7.1.1.9

Activating Compound

Activating Compound Comment Organism Structure
additional information synthetic models of the active site of cytochrome c oxidase [(LN4-OH)CuI-FeII(TMP)]+ and [(LN3-OH)CuI-FeII(TMP)]+ synthetic construct

Metals/Ions

Metals/Ions Comment Organism Structure
Cu reduction of dioxygen to water takes place at the heme a3-CuB binuclear center synthetic construct
Fe2+
-
 synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information oxygenation of the tetradentate model both in MeCN and in other solvents produces a low-temperature-stable dioxygen-bridged peroxide with an O-O stretching vibration at 799 cm-1. Oxygenation of the tridentate model in EtCN solution generates a heme superoxide species with the copper moiety oxidized to copper(II). Coexistence of a heme superoxide and a bridged peroxide species in equivalent amounts when the oxygenation reaction is carried out in CH2Cl2/7% EtCN synthetic construct ?
-
 ?

Synonyms

Synonyms Comment Organism
CCO
-
 synthetic construct
cytochrome c oxidase
-
 synthetic construct

Cofactor

Cofactor Comment Organism Structure
heme reduction of dioxygen to water takes place at the heme a3-CuB binuclear center synthetic construct