Open AccessNMR studies of the heme pocket conformations of monomeric hemoglobins from Glycera dibranchiata
Author(s) -
COOKE Robert M.,
DALVIT Claudio,
NARULA Surinder S.,
WRIGHT Peter E.
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13529.x
Subject(s) - heme , chemistry , histidine , ligand (biochemistry) , hemoglobin , stereochemistry , monomer , steric effects , crystallography , carbon monoxide , hemeprotein , side chain , nuclear magnetic resonance spectroscopy , myoglobin , amino acid , biochemistry , enzyme , catalysis , receptor , polymer , organic chemistry
Two‐dimensional 1 H‐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.