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Literature summary for 1.11.1.5 extracted from

  • Martins, D.; Kathiresan, M.; English, A.M.
    Cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense (2013), Free Radic. Biol. Med., 65C, 541-551.
    View publication on PubMed
Search for more literature for 1.11.1.5

Protein Variants

Protein Variants Comment Organism
additional information generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells Saccharomyces cerevisiae
W191F catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial intermembrane space
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 Saccharomyces cerevisiae 5758
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mitochondrion Ccp1 Saccharomyces cerevisiae 5739
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-
Saccharomyces cerevisiae BY4741
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme partially by preparation of mitochondria Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
CCP1
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 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1 Saccharomyces cerevisiae
additional information resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview Saccharomyces cerevisiae
physiological function cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview Saccharomyces cerevisiae