ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2013
Determination of the principal g-values of Type I or highly-anisotropic low spin (HALS) ferriheme centers in frozen solutions.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Low-frequency EPR of ferrimyoglobin fluoride and ferrimyoglobin cyanide: a case study on the applicability of broadband analysis to high-spin hemoproteins and to HALS hemoproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
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Abstract
Continuous wave (CW) electron paramagnetic resonance (EPR) spectroscopy of highly-anisotropic low spin (HALS) ferric heme centers in frozen solutions is not a very informative approach because usually only one feature is reliably observed in the spectra, that at the maximal principal g-value of, typically, 3.3-3.79. The other two EPR turning points are severely broadened by g-strain and are not easily observed in the first-derivative CW EPR spectra. In this work, we have explored the potential of alternative EPR techniques, the electron spin echo (ESE) field sweep and electron spin transient nutation (TN), for obtaining information about the g-tensors of such systems, using as an example a typical HALS ferric heme center, [Fe(III)((15)N-coproporphyrin)(CN)2]. The analysis of the experimental g-tensor of [Fe(III)((15)N-coproporphyrin)(CN)2](-) has shown that the widths of the underlying energy distributions for this HALS center are comparable to those found for the rhombic bis-imidazole complex. The greater effect on the g-value distributions for HALS centers is determined by near degeneracy of two of the three lower-energy d-orbitals, d(yz) and d(xz), which contain the unpaired electron.
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