Understanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism*

HIGHLIGHTS

• who: Warintra Pitsawong from the Warintra Pitsawong, John PHoben, and Anne-Frances Miller, From the Department of Chemistry, University of Kentucky, Lexington, Kentucky, Background: Nitroreductase reduces a broad range of nitroaromatics. Results: Steady-state and pre-steady-state kinetics were combined with tests for aminoaromatic product formation. Conclusions: Both half-reactions occur via a simple mechanism lacking detectable gating steps consistent with the broad substrate repertoire. Significance: Nitroreductase does not generate p-aminobenzoic acid and, therefore, appears not to reduce nitro groups to amines. The oxygen-insensitive nitroreductase from Enterobacter cloacae (NR) catalyzes two-electron reduction of . . .
  

   

  

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