Abstract
The 57Fe chemical shift of sperm whale carbonyl myoglobin and two model complexes have been determined by double resonance methods in doubly enriched [ 57Fe, 13C] samples. Deprotonation of the axial imidazole in the model complex causes a large upfield 57Fe chemical shift, consistent with the increased ligand field strength. The 57Fe signal for MbCO is to low field of that of the neutral imidazole complex, arguing against significant hydrogen-bonding of its imidazole but supporting a slight axial strain. This indirect method permits the first effective study of 57Fe shifts in a limited class of hemoproteins.
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