The crystal state binding of dithionite to deoxy-hemoglobin

The crystal state binding of sodium ditbionite to deoxyhemoglobinis reported. Dithionite has been used extensively to deoxygenatehemoglobin and myoglobin and there has been considerable interestamong users of dithionite about its effect on protein structureand binding site(s). We have determined that dithionite bindsto deoxygenated hemoglobin crystals at the interface of twomolecules in the crystal lattice. Specific residues involvedin hydrogen bonds or salt interactions with dithionite includeHisll6 and Hisll7 of the ft subunit and Lysl6 of the ß₂subunit of the adjacent hemoglobin molecule. No binding wasobserved at the symmetry related Hisll6 and 117 ß1 residues.We have shown that dithionite does not affect the native hemoglobinstructure or the binding of several allosteric inhibitors tohemoglobin and can be used to mount T state crystals in theair