title: Binding of 2-formylpyridine monothiosemicarbazonato copper II to cat and normal human hemoglobins.
abstract: 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.
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000378:metabolism*; D002415:Cats; D004121:Dimethyl Sulfoxide; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D009942:Organometallic Compounds / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism
chemical_list: D000970:Antineoplastic Agents; D006454:Hemoglobins; D009942:Organometallic Compounds; D006418:Heme; C031471:2-formylpyridine thiosemicarbazonato copper(II); D010100:Oxygen; D004121:Dimethyl Sulfoxide