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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Sep;69(9):2396–2399. doi: 10.1073/pnas.69.9.2396

Study of an Oxygenated Heme Complex in Frozen Solution by Mössbauer Emission Spectroscopy

Linda Marchant *, Michael Sharrock †, Brian M Hoffman *, Eckard Münck †
PMCID: PMC426948  PMID: 4341692

Abstract

We have used Mössbauer emission spectroscopy to study an oxygenated heme complex, produced in a frozen solution by nuclear decay from the isomorphous 57Co-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: oxygen binding, hemoglobin, Co(II)-protoporphyrin IX

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bearden A. J., Moss T. H., Caughey W. S., Beaudreau C. A. Mössbauer spectroscopy of heme and hemin compounds. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1246–1253. doi: 10.1073/pnas.53.6.1246. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Eicher H., Trautwein A. Electronic structure and quadrupole splittings of ferrous iron in hemoglobin. J Chem Phys. 1969 Mar 15;50(6):2540–2551. doi: 10.1063/1.1671413. [DOI] [PubMed] [Google Scholar]
  3. Hoffman B. M., Petering D. H. Coboglobins: oxygen-carrying cobalt-reconstituted hemoglobin and myoglobin. Proc Natl Acad Sci U S A. 1970 Oct;67(2):637–643. doi: 10.1073/pnas.67.2.637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Stynes H. C., Ibers J. A. Thermodyanamics of the reversible oxygenation of amine complexes of cobalt(II) protoporphyrin IX dimethyl ester in a nonagueous medium. J Am Chem Soc. 1972 Mar 8;94(5):1559–1562. doi: 10.1021/ja00760a021. [DOI] [PubMed] [Google Scholar]
  5. Trautwein A., Eicher H., Mayer A., Alfsen A., Waks M., Rosa J., Beuzard Y. Modification of the electronic structure of ferrous iron in hemoglobin by ligandation and by alterations of the protein structure inferred from Mössbauer measurements. J Chem Phys. 1970 Aug 1;53(3):963–967. doi: 10.1063/1.1674164. [DOI] [PubMed] [Google Scholar]
  6. WEISS J. J. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN. Nature. 1964 Apr 4;202:83–84. doi: 10.1038/202083b0. [DOI] [PubMed] [Google Scholar]
  7. WEISS J. J. NATURE OF THE IRON-OXYGEN BOND IN OXYHAEMOGLOBIN. Nature. 1964 Jul 11;203:182–183. [PubMed] [Google Scholar]
  8. Wittenberg J. B., Wittenberg B. A., Peisach J., Blumberg W. E. On the state of the iron and the nature of the ligand in oxyhemoglobin. Proc Natl Acad Sci U S A. 1970 Dec;67(4):1846–1853. doi: 10.1073/pnas.67.4.1846. [DOI] [PMC free article] [PubMed] [Google Scholar]

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