Binding of 2-formylpyridine monothiosemicarbazonato copper II to cat and normal human hemoglobins.

The antitumor agent 2-formylpyridine monothiosemicarbazonato copper(II) forms adducts with sulfur and nitrogen donor atoms from cat hemoglobin but only nitrogen donor atoms from human hemoglobin. Improved resolution of the mI = 1/2 lines in the g parallel region at S-band not only confirms the number of nitrogen donor atoms in the square planar configuration but provides evidence for strong coupling from a proton. Adduct formation results in an increase in the oxygen affinity of hemoglobin. Thus, it is suggested that allosteric enzyme inhibition may be a mechanism for the action of this agent.