Transport of sugars and amino acids in bacteria. XIV. Preferential inhibition of oxidase activities and active transport reactions for amino acids by azidebenzenes.

4-Methylazidebenzene and various azidebenzene derivatives were prepared, and the effects of these compounds on oxidase activities and active transport reactions for amino acids in Escherichia coli cells were studied. Azidebenzenes inhibited succinate oxidation by intact cells preferentially to glycerol oxidation. However, the azidebenzenes could not inhibit succinate oxidation which was not coupled to phosphorylation. The compounds inhibited succinate driven proline uptake much more strongly than isoleucine uptake. Unlike sodium azide and diphenyl phosphorazidate, azidebenzenes did not inhibit membrane-bound, Mg2+-requiring ATPase [EC 3.6.1.3] of E. coli. Reactivities of various azide compounds in the mechanism of inhibition for energy transducing and energy transforming reactions were discussed briefly.