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• W2012509980 abstract "The magnetic circular dichroism (MCD) spectrum of bis-imidazole ferrous tetraphenylporphyrin in the Soret region is nearly the mirror image of the spectrum of ferrous cytochrome b5, a bis-imidazole (histidine)-ligated hemoprotein. Based on previous MCD studies of model and protein heme systems, a sign inversion in the spectra of two heme chromophores having essentially the same coordination structure is unexpected. To investigate whether the nature of the porphyrin itself could account for the observed spectral discrepancy, two additional model complexes, bis-imidazole ferrous protoporphyrin IX dimethylester and bis-imidazole ferrous octaethylporphyrin, whose peripheral porphyrin substituent patterns more closely match that of the protein- bound porphyrin, have been prepared and their MCD spectra measured. In these cases, the band pattern of the ferrous protein in the Soret region is successfully reproduced. It therefore appears that the anomalous MCD spectrum of the tetraphenylporphyrin complex can be attributed to the nature and positioning of the peripheral substituents on the porphyrin ring. Although iron tetraphenylporphyrin complexes are frequently used as models for protoporphyrin- containing hemoproteins, one should be aware that such differences in the peripheral porphyrin substituents may significantly affect the spectral properties of the model complex." @default.
• W2012509980 created "2016-06-24" @default.
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• W2012509980 date "1986-02-01" @default.
• W2012509980 modified "2023-09-26" @default.
• W2012509980 title "Models for ferrous cytochrome b5: Sign inversions in the magnetic circular dichroism spectra of bis-imidazole ferrous porphyrin systems" @default.
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• W2012509980 doi "https://doi.org/10.1016/s0020-1693(00)84305-4" @default.
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