Abstract
A new approach is proposed to provide ultimate answers to such problem as the affinity difference between individual α- and β-subunits in different conformational forms of tetrameric hemoglobin. The approach is based on determination of the bimolecular association rate constant for O 2 rebinding and the apparent quantum yield of photodissociation from single flash photolysis experiment. The potential of the approach is demonstrated with α- and β-subunits within human hemoglobin in the R-state.
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