2-Allyl-2-isopropylacetamide and other drugs containing either an allyl, a vinyl or an ethynyl unsaturated side chain are metabolized by liver cytochrome P-450 to reactive derivatives that irreversibly inhibit the haemoprotein by a suicidal type of inactivation. The main target is the haem moiety of cytochrome P-450 which is converted into abnormal porphyrins. These have been isolated from the liver of treated rats, extensively purified and compared with model porphyrins. The abnormal porphyrins incorporate metal ions in vitro much more readily than does their parent porphyrin, protoporphyrin. They are also much more basic than protoporphyrin, and on titration with a strong acid they readily give rise to a porphyrin monocation which then requires relatively large amounts of acid for conversion to the porphyrin dication. In all these respects and also in the intensity of their bathochromic shifts these abnormal porphyrins closely resemble N-alkylated porphyrins and they markedly differ from porphyrins that are substituted at one of their meso-carbon positions or which bear electron-withdrawing substituents at the beta-positions of the pyrrole rings. This suggests strongly that reactive derivatives of the unsaturated drugs act as electrophilic reagents and alkylate one of the pyrrole nitrogen atoms of cytochrome P-450. A model centred on the apoprotein of cytochrome P-450 is considered for the degradation of liver haem caused by unsaturated drugs. The apocytochrome may accept exchangeable pools of liver haem for degradation, leading to a state of haem depletion and to activation of delta-aminolaevulinate synthase.