The binding of isocyanides to cytochrome P-450 from mouse hepatic microsomes.

The spectral interactions of a number of isocyanides with cytochrome P-450 were investigated. An interaction between the hydrophobic nature of the side chain and the spectral interaction was apparent. The concentration of the isocyanide affected the stability of the complex. Phenyl isocyanide dichloride was determined to be an acceptable replacement for ethyl isocyanide for the characterization of cytochrome P-450.