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Literature summary extracted from

  • Spolitak, T.; Dawson, J.H.; Ballou, D.P.
    Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants (2008), J. Biol. Inorg. Chem., 13, 599-611.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.15.1 cumene hydroperoxide considerable amount of the putative Cpd II species accumulates, even at pH 7.4. By contrast, reactions with meta-chloroperbenzoic acid at pH 7.4 yield very little of the ca. 420 nm species, unless methanol is included Pseudomonas putida
1.14.15.1 methanol reaction with meta-chloroperbenzoic acid in the presence of methanol (3% or ca. 1 M after mixing) at pH 7.4 and 25°C results in the accumulation of a considerable fraction of the P450cam as the putative Cpd II species Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 additional information in contrast to the wild-type, the more hydrophobic sites of the Tyr-to-Phe variants, compared to that of wild-type, favor homolysis more strongly and lead to considerable fractions of the Cpd II like species in reactions with peracids, especially at higher pH Pseudomonas putida
1.14.15.1 Y75F reaction with meta-chloroperbenzoic acid at 25°C, pH 8.0, is similar to that with the Y96F variant, although slightly more Cpd I (and possibly some Cpd ES) is present Pseudomonas putida
1.14.15.1 Y96F reaction with peracetic acid at pH 8.0, 25°C, is similar to that with meta-chloroperbenzoic acid, except that even with 2.4 mM peracetic acid, all steps are slower than those with 0.150 mM meta-chloroperbenzoic acid Pseudomonas putida
1.14.15.1 Y96F/Y75F mutants produce changes in hydrogen bonding patterns and increase hydrophobicity that affect the ratio of heterolytic to homolytic pathways in reactions with cumene hydroperoxide, resulting in a shift of this ratio from 84/16 for wild-type to 72/28 for the Y96F/Y75F double mutant Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Iron
-
 Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-camphor + O2 + reduced putidaredoxin the Cpd II-like species is ineffective at hydroxylating camphor, but can be readily reduced by ascorbate to ferric P450cam, which can then bind camphor to form the high-spin heme Pseudomonas putida exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?
1.14.15.1 peracetic acid + O2 + reduced putidaredoxin
-
 Pseudomonas putida ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.1 cytochrome p450cam
-
 Pseudomonas putida
1.14.15.1 P450cam
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 cytochrome state of cytochrome that is two equivalents of oxidation greater than the ferric form (Cpd I species), state of cytochrome that is one equivalent of oxidation greater than the ferric form (Cpd II species), two-electron-oxidized state of P450 or peroxidases containing both an oxoferryl center [FeIV=O] and either a tryptophanyl or tyrosyl radical, analogous to Cpd ES in cytochrome c peroxidase (Cpd ES species) Pseudomonas putida
1.14.15.1 putidaredoxin
-
 Pseudomonas putida