A comparison of the iron bonding in anhydrohemoglobin and anhydromyoglobin

Mössbauer effect measurements show that the ferrous ions in dehydrated deoxymyoglobin are in the high spin state while those in dehydrated deoxyhemoglobin (AHb) are equally distributed between high and low spin states. It is concluded that the two spin states present in AHb are associated with the iron site difference of the alpha- and beta-chains.