Emission Mössbauer study of the stereochemical trigger that initiates cooperative interaction of hemoglobin subunits.

An important feature of Perutz's trigger mechanism for cooperativity in the reversible oxygenation of hemoglobin (Hb) is the tension along the histidine--metal linkage in deoxyHb and deoxycobaltohemoglobin (deoxy CoHb), supposedly due to the pull exerted by the globin on the metal atom. We have attempted to verify the existence of this pull by studying the emission Mössbauer spectra of deoxy 57CoHb and oxy 57 CoHb at different temperatures. The emission Mössbauer spectrum for none of the cobalt Hbs agrees with the absorption spectrum of the corresponding iron analog and, moreover, the spectrum of deoxy 57CoHb is characteristic of the intermediate-spin iron. These observations indicate that the daughter 57Fe atom is "frozen" almost in the same spatial situation as that of the parent 57Co. The protein is apparently holding the cobalt atom in position rather rigidly and, after the electron-capture decay of the 57Co atom, the protein does not permit the daughter 57Fe to move to a position characteristic of the iron atom.