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On the nature of oxoiron (IV) intermediate in dioxygen activation by non-heme enzymes

  1. Author:
    Nemukhin, A. V.
    Topol, I. A.
    Cachau, R. E.
    Burt, S. K.

  2. Author Address

    NCI, Adv Biomed Comp Ctr, Frederick, MD 21702 USA. Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119992, Russia. Russian Acad Sci, Inst Biochem Phys, Moscow 119997, Russia Topol, IA, NCI, Adv Biomed Comp Ctr, Frederick, MD 21702 USA
    1. Year: 2006
    2. Date: MAY
  2. Journal: Theoretical Chemistry Accounts
    1. 115
    2. 5
    3. Pages: 348-353
  4. Type of Article: Article
  1. Abstract:

    We discuss electronic properties of the molecular systems with the short distance Fe-O unit, which are presumably formed as reaction intermediates during oxygen activation by non-heme enzymes. By performing an analysis of electronic densities in terms of multiconfigurational expansions of wavefunctions with localized orbitals the electronic properties of the Fe-O moiety in two model complexes are compared. The first one refers to the enzymatic intermediate, and the second biomimetic complex models a synthetic compound [Fe(O)(TMC)(NCCH3)](OTf)(2) with a terminal Fe-O unit, which is experimentally characterized as the Fe(IV)=O species. We show that the orbital pictures of the FeO unit in both model complexes share common features. According to these simulations, the non-heme enzymatic intermediates may be assigned to the systems with the oxidation state of Fe between III and IV, as recently proposed for the TauD enzyme in experimental spectroscopic studies

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  2. WOS: 000237562500002

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