Fe-O2 bonding and oxyheme structure in myoglobin.
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...
| Main Authors: | , , |
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| Format: | Text |
| Language: | English |
| Published: |
1978
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| Subjects: | |
| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC392538 http://www.ncbi.nlm.nih.gov/pubmed/276871 |
| Summary: | 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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