Abstract
A series of theoretical approaches, including conventional FF03 and FF03-based polarization model, as well as the generalized energy-based fragmentation (GEBF) quantum chemistry method, have been applied to investigate the interactions between acetate ion (CH3COO−) and the α-subunit of human adult hemoglobin (designated as Hb-α) at four binding sites (Lys16, Lys90, Arg92, and Lys127), respectively. The FF03-based polarizable force fields show that the interaction energies between the CH3COO− group and Hb-α follow the trend of Arg92 > Lys127 > Lys90 > Lys16. The complexation of CH3COO− with Hb-α is governed by the long-range electrostatic interactions and steric effect.
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