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   <subfield code="a">The interaction of heme-free α (αo) and heme-containing β (βh) chains of human hemoglobin has been monitored in 0.1 M potassium phosphate buffer, pH 7 or 8, at [5°C. Soret zero and first-derivative spectra were consistent with a uniform association reaction. Stopped-flow investigations demonstrated association rates on the order of 107 M−1 s−1. This was 100-fold more rapid than the reported rate of combination of αh and βh proteins. This encounter-like rate of semi-β-hemoglobin (αoβh) formation was increased by raising the pH from 7 to 8. pH change is known to affect the spatial arrangement of AB—GH helical entities. Molecular graphic analysis of modeled αo protein superimposed over native αh protein revealed an apo Mb-like structure with well-defined AB—GH segments. Repositioning of these core helical segments, resulting in increased conformational freedom of the α1β1 interface, was apparently responsible for the enhanced association properties of the αo protein.</subfield>
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