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Literature summary for 1.11.1.5 extracted from

  • Echalier, A.; Brittain, T.; Wright, J.; Boycheva, S.; Mortuza, G.B.; Fueloep, V.; Watmough, N.J.
    Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa (2008), Biochemistry, 47, 1947-1956.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 (DE3) cells Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P14532
-
-

Purification (Commentary)

Purification (Comment) Organism
S-Sepharose column chromatography and Superdex-75 gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + H2O2
-
Pseudomonas aeruginosa ferricytochrome c + H2O
-
?

Synonyms

Synonyms Comment Organism
CCP
-
Pseudomonas aeruginosa
cytochrome c peroxidase
-
Pseudomonas aeruginosa