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The binding characteristics and inhibition kinetics of the fatty acid hydroxylase P-450 BM3 from Bacillus megaterium with imidazolyl carboxylic acids were examined. Findings indicated that these compounds are the most potent inhibitors of P-450 BM3. Data showed evidence for interdomain communication between the heme diflavin domains of the flavocytochrome. Binding of the inhibitors to the P-450 BM3 active site resulted from the binding of either pyridine nucleotide or fatty acid substrates at key catalytic residues.