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Tetraphenyl porphyrin (TPP) and its complexes with Fe3+, Co2+, Cu2+, Zn2+ and Ni2+ inhibited cytochrome P-450-dependent enzymes in rat liver microsomes. Content of cytochrome P-450 was decreased by 27% or 49% depending on the substance administered (TPP or its metal complexes, respectively). N-demethylase was inactivated by about 30%; the rate of aniline p-hydroxylation was decreased by 30-45% depending on the type of the metal complex. But these substances did not affect practically the benz(alpha)pyrene hydroxylase activity. The inhibitory effect of TPP of its metal complexes appears to occur due to activation of lipid peroxidation and of hemoxygenase, which is responsible for biodegradation of hem in cytochrome P-450.
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