Iron Distances in Hemoglobin: Comparison of X-Ray Crystallographic and Extended X-Ray Absorption Fine Structure Studies

A comparison is presented of the structures obtained around the iron atom in deoxyhemoglobin (Hb). The data come from extended x-ray absorption fine structure (EXAFS) studies of the iron, which gave Fe--porphyrin nitrogen distances of 2.06 ± 0.01 angstrom, and from the most recent high-resolution x-...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1987-09, Vol.84 (17), p.6167-6168
Main Authors: Fermi, G., Perutz, M. F., Shulman, R. G.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biophysics
Crystal structure
Crystalline structure
Fine structure
Fundamental and applied biological sciences. Psychology
hemoglobin
Hemoglobins
Iron
Molecular biophysics
Nitrogen
Porphyrins
Protein Conformation
Structure in molecular biology
X-ray crystallography
X-Ray Diffraction
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Summary:A comparison is presented of the structures obtained around the iron atom in deoxyhemoglobin (Hb). The data come from extended x-ray absorption fine structure (EXAFS) studies of the iron, which gave Fe--porphyrin nitrogen distances of 2.06 ± 0.01 angstrom, and from the most recent high-resolution x-ray crystallographic study, which gave exactly the same distance--2.06 ± 0.02 angstrom. The distance of Fe above the plane of the porphyrin nitrogens was 0.38 ± 0.04 angstrom from the crystallographic study; this value is not far from the upper limit of the distances 0.20 ± 0.200.10 angstrom calculated from the EXAFS experiment by triangulation. These distances above the nitrogen plane are shorter than those estimated in the earliest x-ray structures.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.17.6167