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Title: WAXS studies of the structural diversity of hemoglobin in solution.

Specific ligation states of hemoglobin are, when crystallized, capable of taking on multiple quaternary structures. The relationship between these structures, captured in crystal lattices, and hemoglobin structure in solution remains uncertain. Wide-angle X-ray solution scattering (WAXS) is a sensitive probe of protein structure in solution that can distinguish among similar structures and has the potential to contribute to these issues. We used WAXS to assess the relationships among the structures of human and bovine hemoglobins in different liganded forms in solution. WAXS data readily distinguished among the various forms of hemoglobins. WAXS patterns confirm some of the relationships among hemoglobin structures that have been defined through crystallography and NMR and extend others. For instance, methemoglobin A in solution is, as expected, nearly indistinguishable from HbCO A. Interestingly, for bovine hemoglobin, the differences between deoxy-Hb, methemoglobin and HbCO are smaller than the corresponding differences in human hemoglobin. WAXS data were also used to assess the spatial extent of structural fluctuations of various hemoglobins in solution. Dynamics has been implicated in allosteric control of hemoglobin, and increased dynamics has been associated with lowered oxygen affinity. Consistent with that notion, WAXS patterns indicate that deoxy-Hb A exhibits substantially larger structural fluctuations than HbCOmore » A. Comparisons between the observed WAXS patterns and those predicted on the basis of atomic coordinate sets suggest that the structures of Hb in different liganded forms exhibit clear differences from known crystal structure.« less
Authors:
; ; ; ; ; ; ; ; ;  [1] ;  [2] ;  [2] ;  [2] ;  [2]
  1. (Biosciences Division)
  2. (
Publication Date:
OSTI Identifier:
1014007
Report Number(s):
ANL/BIO/JA-70027
Journal ID: 0022-2836; TRN: US201110%%866
DOE Contract Number:
DE-AC02-06CH11357
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Mol. Biol.; Journal Volume: 408; Journal Issue: 2011
Research Org:
Argonne National Laboratory (ANL)
Sponsoring Org:
SC; NIH
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; AFFINITY; CATTLE; CRYSTAL LATTICES; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; FLUCTUATIONS; HEMOGLOBIN; METHEMOGLOBIN; OXYGEN; PROBES; PROTEIN STRUCTURE; SCATTERING