Hemoglobin allosteric transition

Kavanaugh JS, Rogers PH, Arnone A. Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin the T-to-T(high) quaternary transitions. Biochemistry 2005 44 6101-6121. 

Allosteric transitions that control binding and activity (hemoglobin, aspartate trans-carbamoylase)... 

Hemoglobin functions efficiently to meet these requirements. It does so through its allosteric transition between structurally different high-affinity and low-affinity states. Carbon dioxide, protons, and other substances all affect hemoglobin and promote allosteric changes. 

Schachman, H. K., 1988. Can a simple model account for the allosteric transition of aspartate transcarbamoylase J. Biol. Chem. 263 18583-18586. Dickerson, R. E., and Geis, I.,1983. Hemoglobin Structure, Function, Evolution and Pathology. Benjamin Cummings. 

Elber, R., A milestoning study of the kinetics of an allosteric transition Atomically detailed simulations of deoxy Scapharca hemoglobin. Biophysical Journal, 2007,92(9) L85-L87. 

Sixth, the extensive thermodynamic and kinetic studies on dimer-tetramer assembly using various hybrid and mutant hemoglobins carried out by Ackers and co-workers clearly indicate that there are at least three molecular functional states for Hb A during the transition from the deoxy to the oxy state (Smith and Ackers, 1985 Ackers and Smith, 1987 Smith et al., 1987 Daugherty et al., 1991 Ackers et al., 1992). These results are not consistent with a two-structure allosteric description for the oxygenation of Hb A. 

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