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 | Comment | Organism | Structure |
---|---|---|---|
Iron | heme | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
34418 | - |
x * 34418, mass spectrometry | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
CCP | - |
Saccharomyces cerevisiae |
cytochrome c peroxidase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Saccharomyces cerevisiae |
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 |