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Literature summary for 1.14.15.1 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
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Protein Variants

Protein Variants Comment Organism
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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