Abstract
There has been much discussion on the mechanistic basis of the variation of affinity values in heme proteins and model compounds. This has focused on the nature of the axial ligand, distal steric effects, distal polar effects and the enforced doming and ruffling of the porphyrin skeleton (Tetreau et al., 1994). In this communication, the 13C NMR spectra of several carbonmonoxide (99.7% 13C and 11.8% 18O enriched) hemoprotein models with varying polar and steric effects of the distal organic superstructure and constraints of the proximal side are reported. This enables the 57Fe-13C(O) coupling constants and 18O isotope effects on 13C shielding to be measured (Figure 1).
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