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PMID: 4519649 Published · ppublish English Journal Article

Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes.

Hofrichter J, Hendricker DG, Eaton WA

Abstract

Possible orientations of deoxyhemoglobin S molecules within sickle-cell fibers are delimited by polarized absorption measurements on single sickled cells and single crystals of deoxyhemoglobin A. The polarization ratio of cells provides a lower limit for that of an individual fiber and, coupled with the absorption properties of the deoxyhemoglobin molecule, restricts the orientation of the long molecular (x) axis to within 22 degrees of the fiber axis. Adopting the stacked ring model of Finch et al. for the molecular positions and the additional constraint that at least one mutated (beta6) site is part of an intermolecular contact, our optical result requires that the true molecular dyad (y) axis pass through some part of an adjacent molecule in the same ring. This range of orientations for the y axis is approximately perpendicular to those described in existing models and places at least one beta6 residue in position to be part of a contact between molecules in the same ring.

MeSH Terms
Anemia, Sickle Cell/blood Erythrocytes/analysis Hemoglobin, Sickle Hemoglobins, Abnormal Humans Models, Structural Protein Conformation Spectrophotometry
Chemicals
Hemoglobin, Sickle Hemoglobins, Abnormal
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hofrichter J
Hendricker D G
Eaton W A
References (23)
23 references, click to expand
  1. The state of hemoglobin in sickled erythrocytes.
    J Exp Med. 1966 Feb 1;123(2):341-6 PMID: 5905245
  2. Molecular mechanism of red cell "sickling".
    Science. 1966 Jul 8;153(3732):145-9 PMID: 5940355
  3. Electronic spectrum of single crystals of ferricytochrome-c.
    J Chem Phys. 1967 Apr 1;46(7):2533-9 PMID: 6039380
  4. Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution.
    J Mol Biol. 1967 Aug 28;28(1):117-56 PMID: 6051747
  5. The physical state of hemoglobin in sickle-cell anemia erythrocytes in vivo.
    J Exp Med. 1968 Apr 1;127(4):711-4 PMID: 5642466
  6. The fine structure of sickled hemoglobin in situ.
    Blood. 1968 May;31(5):561-79 PMID: 4869055
  7. Molecular pathology of human haemoglobin.
    Nature. 1968 Aug 31;219(5157):902-9 PMID: 5691676
  8. Single-crystal spectra of ferrimyoglobin complexes in polarized light.
    J Chem Phys. 1968 Aug 1;49(3):985-95 PMID: 5679525
  9. Polarized single-crystal absorption spectrum of 1-methyluracil.
    J Chem Phys. 1970 Sep 15;53(6):2164-72 PMID: 5449969
  10. Hemoglobin interaction: modification of solid phase composition in the sickling phenomenon.
    Science. 1970 Jul 24;169(3943):375-7 PMID: 5450369
  11. Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution.
    Nature. 1970 Nov 7;228(5271):551-2 PMID: 5472471
  12. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution.
    J Biol Chem. 1971 Mar 10;246(5):1511-35 PMID: 5545094
  13. Intermolecular organization of deoxygenated sickle haemoglobin determined by x-ray diffraction.
    Nature. 1972 Sep 22;239(5369):217-9 PMID: 4562732
  14. Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers.
    Proc Natl Acad Sci U S A. 1973 Mar;70(3):718-22 PMID: 4123689
  15. Structure of fibers of sickle cell hemoglobin.
    Proc Natl Acad Sci U S A. 1973 Apr;70(4):1104-7 PMID: 4123929
  16. Polarized single crystal absorption spectra of carboxy- and oxyhemoglobin.
    Ann N Y Acad Sci. 1973;206:210-22 PMID: 4356180
  17. State of haemoglobin in sickle-cell anaemia.
    Nature. 1950 Oct 21;166(4225):677-9 PMID: 14780193
  18. Studies on the destruction of red blood cells. VIII. Molecular orientation in sickle cell hemoglobin solutions.
    Proc Soc Exp Biol Med. 1950 Oct;75(1):197-201 PMID: 14797780
  19. Properties of sickle-cell haemoglobin.
    Biochem J. 1957 Feb;65(2):212-9 PMID: 13403895
  20. [Sickling of erythrocytes studied with polarized light & electron microscopes. II. Erythrocyte internal structure; comparison with intra-erythrocytic crystals].
    Rev Hematol. 1958 Apr-Jun;13(2):249-70 PMID: 13568373
  21. STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION.
    Nature. 1963 Aug 17;199:633-8 PMID: 14074546
  22. MOLECULAR ORIENTATION IN HORSE HEMOGLOBIN CRYSTALS AND SICKLED ERYTHROCYTES.
    Biochim Biophys Acta. 1965 Jan 25;94:194-9 PMID: 14275517
  23. Sickle cell anemia a molecular disease.
    Science. 1949 Nov 25;110(2865):543-8 PMID: 15395398
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1973-12-00
Pages
3604-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC427289
Subset
IM
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