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The inhibitory effects of 15 hydrocarbons and halogenated hydrocarbons on NH3 oxidation by ammonia monooxygenase (AMO) in intact cells of the nitrifying bacteriumNitrosomonas europaea were determined. Determination of AMO activity, measured as NO2 - production, required coupling of hydroxylamine oxidoreductase (HAO) activity with NH3 -dependent NH2 OH production by AMO. Hydrazine, an alternate substrate for HAO, was added to the reaction mixtures as a source of reductant for AMO. Most inhibitors exhibited competitive or noncompetitive inhibition patterns. The competitive character generally decreased (Ki E /Ki ES increased) as the molecular size of the inhibitors increased. For example, CH4 and C2 H4 were competitive inhibitors of NH3 oxidation, whereas the remaining alkanes (up to C4 ) and monohalogenated (Cl, Br, I) alkanes were noncompetitive. Oxidation of C2 H5 Br (noncompetitive) increased as the NH4 + concentration increased up to 40 mM, whereas oxidations of inhibitors with competitive character (Ki E ≪Ki ES ) were diminished at 40 mM NH4 + . Multichlorinated compounds produced nonlinear Lineweaver-Burk plots. Iodinated alkanes (CH3 I, C2 H5 I) and C2 Cl4 were potent inhibitors of NH3 oxidation. Maximum rates of NH3 , C2 H4 , and C2 H6 oxidations were approximately equivalent, suggesting a common rate-determining step. These data support an active-site model for AMO consisting of an NH3 -binding site and a second site that binds noncompetitive inhibitors, with oxidation occurring at either site.

applied and environmental microbiology

Kinetic Studies of Ammonia Monooxygenase Inhibition in <i>Nitrosomonas europaea</i> by Hydrocarbons and Halogenated Hydrocarbons in an Optimized Whole-Cell Assay

Kinetic Studies of Ammonia Monooxygenase Inhibition in Nitrosomonas europaea by Hydrocarbons and Halogenated Hydrocarbons in an Optimized Whole-Cell Assay