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      Active species of horseradish peroxidase (HRP) and cytochrome P450: two electronic chameleons.

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          Abstract

          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.

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          Author and article information

          Journal
          J. Am. Chem. Soc.
          Journal of the American Chemical Society
          American Chemical Society (ACS)
          0002-7863
          0002-7863
          Dec 24 2003
          : 125
          : 51
          Affiliations
          [1 ] Department of Organic Chemistry and the Lise Meitner-Minerva Center for Computational Quantum Chemistry, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel.
          Article
          10.1021/ja0380906
          14677968
          8ea85a95-caad-4598-aadf-0cbfb9c7191d
          History

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