Active Species of Horseradish Peroxidase (HRP) and Cytochrome P450: Two Electronic Chameleons

Sam P. De Visser, Sason Shaik, Pankaz K. Sharma, Devesh Kumar, Walter Thiel

    Research output: Contribution to journalArticlepeer-review


    The active site of HRP Compound I (Cpd I) is modeled using hybrid density functional theory (UB3LYP). The effects of neighboring amino acids and of environmental polarity are included. The low-lying states have porphyrin radical cationic species (Por.+). However, since the Por .+ species is a very good electron acceptor, other species, which can be either the ligand or side chain amino acid residues, may participate in electron donation to the Por.+ moiety, thereby making Cpd I behave like a chemical chameleon. Thus, this behavior that was noted before for Cpd I of P450 is apparently much more wide ranging than initially appreciated. Since chemical chameleonic behavior property was found to be expressed not only in the properties of Cpd I itself, but also in its reactivity, the roots of this phenomenon are generalized. A comparative discussion of Cpd I species follows for the enzymes HRP, CcP, APX, CAT (catalase), and P450.
    Original languageEnglish
    Pages (from-to)15779-15788
    Number of pages9
    JournalJournal of the American Chemical Society
    Issue number51
    Publication statusPublished - 24 Dec 2003


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