Skip to main content
NCBI home page
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
. 1969 Jul;63(3):934–939. doi: 10.1073/pnas.63.3.934

HEMOGLOBIN A: AN ELECTRON PARAMAGNETIC RESONANCE STUDY OF THE EFFECTS OF INTERCHAIN CONTACTS ON THE HEME SYMMETRY OF HIGH-SPIN AND LOW-SPIN DERIVATIVES OF FERRIC ALPHA CHAINS*

J Peisach 1,2,3,4,†, W E Blumberg 1,2,3,4, B A Wittenberg 1,2,3,4, J B Wittenberg 1,2,3,4,‡, L Kampa 1,2,3,4
PMCID: PMC223542  PMID: 4310518

Abstract

Hemoglobin, the oxygen-binding heme protein of blood is composed of four subunits of two types, alpha and beta. Although the protein when isolated is diamagnetic, by oxidation it can be converted to various paramagnetic ferric forms exhibiting specific electron paramagnetic resonance (EPR) spectra. Using electron paramagnetic resonance, we have shown that the symmetry of the heme of isolated ferric alpha chains is different from that of the heme of these same subunits when associated with ferric beta chains in the parent tetramer. The high-spin form of the isolated ferric alpha chains shows a clearly resolved departure from tetragonal symmetry in contrast to ferrihemoglobin A, where the environment of the iron of all four chains is nearly tetragonal. This difference in heme symmetry suggests that the maintenance of tetragonal symmetry in the hemoglobin tetramer must be brought about by the configuration the alpha chains assume due to their contact with the beta chains. When isolated from the tetramer, some parts of the alpha chain must undergo physical displacement from a configuration that had been stabilized by the beta chains.

Although differences in symmetry between monomer and tetramer are seen with high-spin forms, no such difference exists with two low-spin ferric forms. Here the symmetries of iron are primarily governed by the immediate ligand environment of the iron and not by the state of association of the protein.

Full text

PDF
934

Selected References

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

  1. Antonini E., Brunori M., Anderson S. Studies on the relations between molecular and functional properties of hemoglobin. VII. Kinetic effects of the reversible dissociation of hemoglobin into single chain molecules. J Biol Chem. 1968 Apr 25;243(8):1816–1822. [PubMed] [Google Scholar]
  2. Blumberg W. E., Peisach J., Wittenberg B. A., Wittenberg J. B. The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives. J Biol Chem. 1968 Apr 25;243(8):1854–1862. [PubMed] [Google Scholar]
  3. GERALD P. S., EFRON M. L. Chemical studies of several varieties of Hb M. Proc Natl Acad Sci U S A. 1961 Nov 15;47:1758–1767. doi: 10.1073/pnas.47.11.1758. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GIBSON J. F., INGRAM D. J., PERUTZ M. F. Orientation of the four haem groups in haemoglobin. Nature. 1956 Oct 27;178(4539):906–908. doi: 10.1038/178906a0. [DOI] [PubMed] [Google Scholar]
  5. Hayashi A., Suzuki T., Shimizu A., Morimoto H., Watari H. Changes in EPR spectra of M-type abnormal haemoglobins induced by deoxygenation and their implications for the haem-haem interaction. Biochim Biophys Acta. 1967 Oct 23;147(2):407–409. doi: 10.1016/0005-2795(67)90426-6. [DOI] [PubMed] [Google Scholar]
  6. Hollocher T. C., Buckley L. M. Electron spin resonance studies of native and denatured methemoglobin. pH effects. J Biol Chem. 1966 Jun 25;241(12):2976–2980. [PubMed] [Google Scholar]
  7. Peisach J., Blumberg W. E., Wittenberg B. A., Wittenberg J. B. The electronic structure of protoheme proteins. 3. Configuration of the heme and its ligands. J Biol Chem. 1968 Apr 25;243(8):1871–1880. [PubMed] [Google Scholar]
  8. SHIMIZU A., HAYASHI A., YAMAMURA Y., TSUGITA A., KITAYAMA K. THE STRUCTURAL STUDY ON A NEW HEMOGLOBIN VARIANT, HB MOSAKA. Biochim Biophys Acta. 1965 Mar 8;97:472–482. doi: 10.1016/0304-4165(65)90159-5. [DOI] [PubMed] [Google Scholar]
  9. STRYER L., KENDREW J. C., WATSON H. C. THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN. J Mol Biol. 1964 Jan;8:96–104. doi: 10.1016/s0022-2836(64)80152-2. [DOI] [PubMed] [Google Scholar]
  10. Shimizu A., Tsugita A., Hayashi A., Yamamura Y. The primary structure of hemoglobin M-Iwate. Biochim Biophys Acta. 1965 Sep 13;107(2):270–277. doi: 10.1016/0304-4165(65)90134-0. [DOI] [PubMed] [Google Scholar]
  11. Watari H., Hwang K. J., Kimura K., Murase K. Electron spin resonance studies of ferrihaemoglobin MOsaka. Biochim Biophys Acta. 1966 May 12;120(1):131–136. doi: 10.1016/0926-6585(66)90284-6. [DOI] [PubMed] [Google Scholar]
  12. Wittenberg B. A., Kampa L., Wittenberg J. B., Blumberg W. E., Peisach J. The electronic structure of protoheme proteins. II. An electron paramagnetic resonance and optical study of cytochrome c peroxidase and its derivatives. J Biol Chem. 1968 Apr 25;243(8):1863–1870. [PubMed] [Google Scholar]
  13. Yonetani T., Schleyer H. Electromagnetic properties of hemoproteins. I. Electron paramagnetic resonance absorptions of single crystals of ferrimyoglobin and cytochrome c peroxidase. J Biol Chem. 1967 Sep 10;242(17):3919–3925. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES