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Literature summary for 1.11.1.5 extracted from

  • DiCarlo, C.M.; Vitello, L.B.; Erman, J.E.
    Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pH (2011), J. Inorg. Biochem., 105, 532-537.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.5

Protein Variants

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

Metals/Ions Comment Organism Structure
Iron Fe(III) reduction to Fe(IV) in heme cofactor Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae Red Star
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
cytochrome c peroxidase
-
 Saccharomyces cerevisiae

Cofactor

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

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