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  • Title: Correlations among parameters that describe low-spin ferric heme complexes.
    Author: Muhoberac BB.
    Journal: Arch Biochem Biophys; 1984 Sep; 233(2):682-97. PubMed ID: 6091554.
    Abstract:
    The g values from low-spin ferric hemes can be related through the t2g hole model to rhombic (V/lambda) and tetragonal (delta/lambda) ligand field components and to the lowest Kramer's doublet energy (E/lambda). The latter is also a measure of unpaired electron sharing among the iron 3d (t2g) orbitals. For a series of ligands (X), there is a monotonic increase in myoglobin complex (Mb . X) [E/lambda] values with nonheme hexacoordinate metal complex (M . X6) [eg-t2gPg] orbital separations. As the aqueous solution pKa values of the sulfurous or nitrogenous ligands in model heme complexes increase, values of V/lambda and delta/lambda increase linearly, but those of [E/lambda] decrease linearly. The greater the electron-acceptor ability of the ligand, as suggested by its position in the spectrochemical series or its pKa, the more the unpaired electron sharing among the heme t2g orbitals increases. The rate of change of [E/lambda] with V/lambda and the pKa is different with sulfurous and nitrogenous ligands, and the magnitude of both rates increases with two sulfurs less than sulfur and nitrogen less than two nitrogens bound to the heme. The maximum magnitude of this rate with V/lambda for cytochrome P-450 is four times less than that for myoglobin, which may explain, in part, the differences in ligand binding between these two hemeproteins. The perturbation of [E/lambda], V/lambda, and delta/lambda induced by strain of iron-ligand bonds is quantitated for several hemeproteins and heme models. In addition, energy level comparisons suggest that the largest-magnitude g value falls approximately along the iron-chlorin ring normal. This suggestion implies that the electron distribution of the iron at the catalytic sites of cytochrome P-450 and certain chlorin-containing enzymes is in some way similar, but distinct from that at the transport site of myoglobin.
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