Abstract
A series of 2-arylalkyl- and 2-(4''-alkyl)phenoxymethylbenzimidazoles was synthesized and evaluated as inhibitors of mixed-function oxidase activity in phenobarbitone- and .beta.-naphthoflavone-induced rat liver microsomes. Higher homologues of the 2-arylakyl series were more potent inhibitors than lower homologues against all monooxygenase activities except aniline p-hydroxylation. Smaller 2-substituents were associated with relatively low-affinity reverse type 1 spectral binding behavior; larger substituents were associated with type 1 of high affinity binding.

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