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Literature summary extracted from

  • Song, A.X.; Li, L.Z.; Yu, T.; Chen, S.M.; Huang, Z.X.
    Role of tryptophan 121 in the soluble CuA domain of cytochrome c oxidase: structure and electron transfer studies (2003), Protein Eng., 16, 435-441.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.9 wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L are expressed in Escherichia coli BL21 Paracoccus versutus

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.9 DELTAW121 mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely Paracoccus versutus
7.1.1.9 W121L mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely Paracoccus versutus
7.1.1.9 W121Y mutant of the soluble CuA domain, stability decreases compared with the wild-type enzyme. The mutant keeps the same secondary structure as the wild-type protein, but can only transfer electrons with cytochrome c at a rate of one-seventh-fold Paracoccus versutus

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Paracoccus versutus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.9 wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L, expressed in Escherichia coli Paracoccus versutus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2
-
 Paracoccus versutus ferricytochrome c + H2O
-
 ?