Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure.
Cyanomet human hemoglobin has been crystallized at a chloride ion concentration and pH similar to physiological conditions. Molecular replacement calculations definitively show that the hemoglobin subunits are arranged in the Y quaternary form recently discovered in carbon monoxy hemoglobin Yp-silanti (beta 99 Asp-Tyr), and subsequently observed in carbon monoxy normal human hemoglobin crystallized at low ionic strength and low pH. The structure has been refined at 2.09 A resolution to an R-value of 0.232, and further refinement is currently underway. Although the refinement is not yet complete, our results are the first indication that the Y structure may represent an important quaternary form of liganded hemoglobin under physiological buffer conditions. These results suggest the need for a reexamination of structure-function correlations in the hemoglobin system.
Smith
F R
FR
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill 27599-7260.
Simmons
K C
KC
D002021:Buffers; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D008706:Methemoglobin / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation
D002021:Buffers; D008024:Ligands; C007169:cyanomethemoglobin; D008706:Methemoglobin