Heme proteins, Mossbauer spectroscop

Mossbauer spectroscopic measurements suggest that the hydration water of myoglobin and the internal motions of the protein are coupled. [ Fe]Ferricyanide diffused into the solvent of myoglobin crystals exhibits (x ) values equal to those for the heme iron for temperatures below 250 K, and greater than those for the heme iron at higher temperatures (50% greater at 300 K) (Parak, 1986). The [ Fe]ferricyanide in the crystal monitors motions of the hydration water [ Fe]ferricyanide in bulk water shows no Mossbauer spectrum. 

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