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Structural consequences of heme isomerism in monomeric hemoglobins from glycera-dibranchiata

Academic Article
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Overview

authors

  • Cooke, R. M.
  • Wright, Peter

publication date

  • July 1987

journal

  • European Journal of Biochemistry  Journal

abstract

  • Two-dimensional 1H-NMR methods have been used to assign heme and amino acid proton resonances in both isomeric states of the carbon monoxide complexes of two Glycera dibranchiata monomeric hemoglobins, HbA and HbB. For each hemoglobin, there are small differences in heme pocket structure in the two isomeric forms. The largest structural perturbations associated with heme isomerism involve residues close to pyrrole rings I and II. The positions relative to the heme of phenylalanine CD1 and the proximal histidine ligand are almost unaffected by heme isomerism. These residues probably play a key role in determining the location of the heme within the heme pocket.

subject areas

  • Animals
  • Heme
  • Hemoglobin A
  • Hemoglobins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Polychaeta
  • Protein Conformation
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1987.tb13530.x

PubMed ID

  • 3609018
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Additional Document Info

start page

  • 409

end page

  • 414

volume

  • 166

issue

  • 2

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