Alkyl and aromatic isocyanide binding to haem complexes.

Equilibrium constants for the binding of ethyl (EIC), n-butyl (BIC), p-toluenesulphonylmethyl (TMIC) and 2,6-dimethylphenyl isocyanides (DIMPI) to an imidazole-haem complex in toluene and aqueous detergent micelle solutions were determined. In contrast to an earlier study, which indicated that the large affinities of myoglobin for binding DIMPI and 2,6-diethylphenylisocyanide (DEPI) relative to EIC were due to an electronic effect, the present study shows a similarity in binding constants for EIC, BIC, and DIMPI to the imidazole-haem complex in toluene, suggesting no such electronic effect is present. The measured hydrophobic effect (KDIMPI/KEIC = 11) cannot account for the large binding constant reported for DIMPI relative to the binding of EIC to myoglobin. Based on the results of these model studies, the equilibrium binding constant for DIMPI to myoglobin has been re-measured and the standard free energy of binding has been analysed by a more recent method.