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Literature summary extracted from

  • Wang, B.; Li, C.; Dubey, K.D.; Shaik, S.
    Quantum mechanical/molecular mechanical calculated reactivity networks reveal how cytochrome P450cam and its T252A mutant select their oxidation pathways (2015), J. Am. Chem. Soc., 137, 7379-7390 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 T252A mutant displays an additional coupling pathway responsible for the epoxidation of 5-methylenylcamphor. During the reaction, camphor cannot prevent H2O2 release and hence the T252A mutant does not oxidize camphor Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida P00183
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 additional information an additional coupling pathway transpires during H2O2 shunting of the cycle of wild-type P450cam and in mutant T252A. The reaction starts with the FeIII(O2H2) intermediate, which transforms to Cpd I via a O-O homolysis/H-abstraction mechanism. The substrate 5-methylenylcamphor prevents H2O2 release, while the protein controls the FeIII(O2H2) conversion to Cpd I by nailing through hydrogen-bonding interactionsthe conformation of the HO radical produced during O-O homolysis. This conformation prevents HO readical attack on the porphyrin’s meso position, as in heme oxygenase, and prefers H-abstraction from FeIVOH thereby generating H2O + Cpd I. Cpd I then performs substrate oxidations Pseudomonas putida ?
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