Fe-O2 bonding and oxyheme structure in myoglobin.
- 1 May 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (5) , 2291-2295
- https://doi.org/10.1073/pnas.75.5.2291
Abstract
In the polarized electronic absorption spectrum of oxymyoglobin in single crystals, charge-transfer states involving orbitals of the Fe and O2 ligand are defined as probes of oxyheme orbital structure and coordination geometry. The spectrum of sperm whale oxymyoglobin is diagnostic of a bent .**GRAPHIC**. oxyheme coordination geometry with totally spin-paired, ground-state electronic configurations of the Fe 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.This publication has 27 references indexed in Scilit:
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