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. 1972 Oct;69(10):2783–2787. doi: 10.1073/pnas.69.10.2783

Electron Paramagnetic Resonance of Single Crystal Oxycobaltmyoglobin and Deoxycobaltmyoglobin

James C W Chien 1, L Charles Dickinson 1
PMCID: PMC389644  PMID: 4342964

Abstract

Single crystals of oxycobaltmyoglobin and deoxycobaltmyoglobin have been prepared and found to be isomorphous. The paramagnetic resonance spectra of deoxycobaltmyoglobin yield gxx = 2.330, gyy = 2.323, gzz = 2.028 with the z-axis parallel to the “heme” normal. The ACo and g tensors share the same principal axes with|ACo∥| = 79 G and|ACo[unk]| = 6 G. A value of AN = 17.5 G was also obtained for the ε-N atom of the F8 histidine. There are two paramagnetic species in oxycobaltmyoglobin having apparently identical g-tensors (gξξ = 2.083, gηη = 2.006, and gζζ = 1.989) but different ACo-tensors. Furthermore, g values ACo do not share the same principal axes. The ACo-values for one of the species are (Axx = 16.7 G, Ayy = 5.95 G, Azz = 9.3 G), they are all 40% larger for the other species. The two species are oriented 90° to each other in the crystal. The results from electron paramagnetic resonance studies are consistent with a π-bounded structure for CoMbO2.

Keywords: sperm-whale myoglobin, apomyoglobin, paper electrophoresis

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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