Protein Variants | Comment | Organism |
---|---|---|
H52L | | site-directed mutagenesis, a distal pocket mutant | Saccharomyces cerevisiae |
H52Q | | site-directed mutagenesis, a distal pocket mutant | Saccharomyces cerevisiae |
additional information | pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview | Saccharomyces cerevisiae |
R48L/W51L/H52L | | site-directed mutagenesis, a distal pocket mutant | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | Fe(III) reduction to Fe(IV) in heme cofactor | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome c + H2O2 | Saccharomyces cerevisiae | - |
2 ferricytochrome c + 2 H2O | - |
? | |
2 ferrocytochrome c + H2O2 | Saccharomyces cerevisiae Red Star | - |
2 ferricytochrome c + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Saccharomyces cerevisiae Red Star | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome c + H2O2 | - |
Saccharomyces cerevisiae | 2 ferricytochrome c + 2 H2O | - |
? | |
2 ferrocytochrome c + H2O2 | - |
Saccharomyces cerevisiae Red Star | 2 ferricytochrome c + 2 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cytochrome c peroxidase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | Fe(III) reduction to Fe(IV) in heme cofactor, pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
additional information | His175 and Asp235 in the proximal heme pocket form another H-bonding cluster that provides a proton-binding site that is responsive to changes in the redox state of the heme iron. Arg-48 is not a good candidate for the proton-binding site. Arg48 interacts with multiple waters, is located near the bottom of the solvent-access channel in CcP. The carboxylate group of heme propionate-7, His181, and Asp37 form a hydrogen-bonded cluster near the heme iron | Saccharomyces cerevisiae |