Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.

@article{Birukou2010DistalHS,
  title={Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.},
  author={Ivan Birukou and Rachel L Schweers and John S Olson},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 12},
  pages={8840-54}
}
The role of the distal histidine in regulating ligand binding to adult human hemoglobin (HbA) was re-examined systematically by preparing His(E7) to Gly, Ala, Leu, Gln, Phe, and Trp mutants of both Hb subunits. Rate constants for O(2), CO, and NO binding were measured using rapid mixing and laser photolysis experiments designed to minimize autoxidation of the unstable apolar E7 mutants. Replacing His(E7) with Gly, Ala, Leu, or Phe causes 20-500-fold increases in the rates of O(2) dissociation… CONTINUE READING
19 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 19 extracted citations

Similar Papers

Loading similar papers…