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Literature summary for 1.11.1.5 extracted from

  • Volkov, A.N.; Wohlkonig, A.; Soror, S.H.; van Nuland, N.A.
    Expression, purification, characterization, and solution nuclear magnetic resonance study of highly deuterated yeast cytochrome C peroxidase with enhanced solubility (2013), Biochemistry, 52, 2165-2175.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
functional expression of deuterated and soluble His-tagged Ccp in Escherichia coli strain BL21(DE3). Introduction of a His-tag at either protein terminus dramatically increases its solubility, allowing preparation of concentrated, stable CcP samples. The engineered His tags neither perturb the structure of the enzyme nor alter the heme environment or its reactivity toward known ligands Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Iron heme Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34418
-
x * 34418, mass spectrometry Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble His-tagged Ccp from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
? x * 34418, mass spectrometry Saccharomyces cerevisiae
More recombinant His-tagged enzyme is used for structure analysis by multidimensional NMR spectroscopy, structure modeling, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
CCP
-
Saccharomyces cerevisiae
cytochrome c peroxidase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
heme
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information the catalytic mechanism of H2O2 reduction involves formation of CcP Compound I (CpdI), an intermediate oxidized 2 equiv above the CcP Fe(III) resting state and containing Fe(IV)=O heme oxyferryl and W191 cation radical. Subsequent CpdI reduction occurs in two one-electron steps, involving complex formation with ferrous Cc, intermolecular electron transfer (ET), and product dissociation Saccharomyces cerevisiae
physiological function CcP catalyzes reduction of hydroperoxides using the electrons provided by its physiological binding partner cytochrome c Saccharomyces cerevisiae