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. 1978 May;75(5):2291–2295. doi: 10.1073/pnas.75.5.2291

Fe-O2 bonding and oxyheme structure in myoglobin.

M W Makinen, A K Churg, H A Glick
PMCID: PMC392538  PMID: 276871

Abstract

In the polarized electronic absorption spectrum of oxymyoglobin in single crystals, charge-transfer states involving orbitals of the iron and dioxygen ligand are defined as probes of oxyheme orbital structure and coordination geometry. The spectrum of sperm whale oxymyoglobin is diagnostic of a bent (formula: see text) oxheme coordination geometry with totally spin-paired, ground-state electronic configurations of the iron and of the dioxygen ligand. In contrast, Aplysia myoglobin is distinguishably different in oxyheme structure, indicating that the geometry of Fe-O2 bonding in heme proteins can be altered by the protein environment.

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Selected References

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