Study of an Oxygenated Heme Complex in Frozen Solution by Mössbauer Emission Spectroscopy
- 1 September 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 69 (9) , 2396-2399
- https://doi.org/10.1073/pnas.69.9.2396
Abstract
We have used Mössbauer emission spectroscopy to study an oxygenated heme complex, produced in a frozen solution by nuclear decay from the isomorphous (57)Co-labeled compound. The Mössbauer parameters agree with those obtained by Mössbauer absorption spectroscopy of oxyhemoglobin. Thus, a nonprotein environment for iron can duplicate the unique oxyhemoglobin Mössbauer spectrum. The electronic structure of the heme iron in oxyhemoglobin is not significantly influenced by the protein environment. Mössbauer emission spectroscopy can be useful in the investigation of heme proteins.Keywords
This publication has 8 references indexed in Scilit:
- Thermodynamics of the reversible oxygenation of amine complexes of cobalt(II) protoporphyrin IX dimethyl ester in a nonaqueous mediumJournal of the American Chemical Society, 1972
- On the State of the Iron and the Nature of the Ligand in OxyhemoglobinProceedings of the National Academy of Sciences, 1970
- Coboglobins: Oxygen-Carrying Cobalt-Reconstituted Hemoglobin and MyoglobinProceedings of the National Academy of Sciences, 1970
- Modification of the Electronic Structure of Ferrous Iron in Hemoglobin by Ligandation and by Alterations of the Protein Structure Inferred from Mössbauer MeasurementsThe Journal of Chemical Physics, 1970
- Electronic Structure and Quadrupole Splittings of Ferrous Iron in HemoglobinThe Journal of Chemical Physics, 1969
- Mössbauer spectroscopy of heme and hemin compounds.Proceedings of the National Academy of Sciences, 1965
- NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN.1964
- Nature of the Iron–Oxygen Bond in OxyhæmoglobinNature, 1964