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  • Iron porphyrin dications with neutral axial ligands: DFT calculations delineate similarities with heme protein compound II intermediates.

Iron porphyrin dications with neutral axial ligands: DFT calculations delineate similarities with heme protein compound II intermediates.

The journal of physical chemistry. B (2011-03-18)
Adam C Chamberlin, Akira Ikezaki, Mikio Nakamura, Abhik Ghosh
ABSTRACT

OLYP/TZP calculations on two symmetrized model complexes [Fe(TPP)(py)(2)](2+) and [Fe(TPP)(PhNC)(2)](2+) (TPP = meso-tetraphenylporphyrin, py = pyridine, PhNC = phenylisocyanide) reveal dense manifolds of low-energy electronic states. For the latter complex, broken-symmetry calculations successfully reproduce the unique S = 0 ground state that is expected on the basis of experimental measurements on a closely related complex; the S = 0 state arises from antiferromagnetic coupling between a low-spin d(xy)(1)(d(xz),d(yz))(4) Fe(III) center and a porphyrin "a(2u)" radical. Furthermore, the calculations indicate low-energy Fe(IV) states for both complexes. Overall, the results contribute to our deepening understanding of the factors contributing to the stability of iron(IV) centers. Thus, a dianionic π-donor oxo ligand is no longer deemed a requirement for the stability of heme-based Fe(IV) centers; iron(IV) intermediates of heme proteins such as chloroperoxidase, catalase, and MauG, having only monanionic ligands such as hydroxide, thiolate, and phenolate and/or (in the case of MauG) a neutral histidine as axial ligands, are now firmly established.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, aqueous suspension, brown, >10,000 U/mL
Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, buffered aqueous suspension, ≥3,000 units/mL
Sigma-Aldrich
Chloroperoxidase from Caldariomyces fumago, buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)