Freezing induced change in ligand orientation in oxycobalt-myoglobin
- 1 December 1980
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 288 (5790) , 501-502
- https://doi.org/10.1038/288501a0
Abstract
Single crystals of oxycobalt-[Sperm Whale] myoglobin were examined by EPR spectroscopy at ambient and cryogenic temperatures. The principal values and eigenvectors of the g-tensor and the hyperfine coupling tensor were determined. The Co.sbd.O.sbd.O bond angle was estimated to be 125.degree. at ambient temperature. The single crystal EPR data of oxycobalt myoglobin at 77.degree. K showed 2 sets of the prinicipal values for g and hyperfine coupling tensors and eigenvectors, indicating that the bound oxygen molecule takes 2 distinct orientations. The well defined change in the molecular orientation is induced upon freezing the biological macromolecule.Keywords
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