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Nmr-studies of the heme pocket conformations of monomeric hemoglobins from glycera-dibranchiata - implications for ligand-binding

Academic Article
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Overview

authors

  • Cooke, R. M.
  • Dalvit, C.
  • Narula, S. S.
  • Wright, Peter

publication date

  • July 1987

journal

  • European Journal of Biochemistry  Journal

abstract

  • Two-dimensional 1H-NMR methods have been used to assign side-chain resonances for the tryptophan residues and for several amino acids located in the heme pockets of the carbon monoxide complexes of the major monomeric hemoglobins from Glycera dibranchiata. The NMR spectra reveal a high degree of conservation of the heme pocket structure in the different hemoglobins. However some conformational differences are evident and residues at positions B10 and G8 on the distal side of the heme pocket are not conserved. From the present NMR studies it appears that the monomeric G. dibranchiata hemoglobin examined by X-ray crystallography [Padlan, E. A. & Love, W. (1974) J. Biol. Chem. 249, 4067-4078] corresponds to HbC. Except that the orientation of the heme in solution is the reverse of that reported in the crystal structure, there is a close correspondence between the heme pocket structure in the crystal and in solution. The proximal histidine coordination geometry is almost identical in the CO complexes of the three monomeric hemoglobins studied. Distal residues are strongly implicated in determining the observed kinetic differences in ligand binding reactions. In particular, steric crowding of the ligand binding site in hemoglobin A is probably a major factor in the slower kinetics of this component.

subject areas

  • Amino Acid Sequence
  • Animals
  • Heme
  • Hemoglobins
  • Magnetic Resonance Spectroscopy
  • 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.tb13529.x

PubMed ID

  • 3609017
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Additional Document Info

start page

  • 399

end page

  • 408

volume

  • 166

issue

  • 2

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