Title : Determination of relative spin concentration in some high-spin ferric proteins using E/D-distribution in electron paramagnetic resonance simulations.

Pub. Date : 1987 Jan

PMID : 3026504






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin. Iron phenylalanine hydroxylase Homo sapiens
2 Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin. Iron phenylalanine hydroxylase Homo sapiens
3 In both PAH and transferrin, at least one of the iron sites is characterized by the ratio of zero-field splitting parameters, E/D, near 1/3 and a broad, asymmetric lineshape. Iron phenylalanine hydroxylase Homo sapiens
4 When applied to spectra of PAH in the resting state, the E/D-distribution approach accounts for the intensity of one of the two major species of iron. Iron phenylalanine hydroxylase Homo sapiens