Intracellular localization and co-factor requirement of nitroreductase in rat liver.

Nuruerous aromatic iii roe rirpounds are reduced to aromatic amines by nianrmalian liver. Bouts and Brodie (1) reported that the nitroreductase was localized in 0•,0(10 x g supernatant of liver. Although both N:A1)PH and NAUH can serve as electron donors, NADPH was about four times more effective:than NADH. I t is known that hydroxylamines are formed as intermediate in the reduction of nitrocompounds to aromatic amines (1, 2). However, many works on the reduction of' litrocompounds were carried out by rneasurin,g the formation of aromatic arnines (1 3). I n the present studies, therefore, the step of nitroreduction was separated into two steps arid the intracel lular localization and co-factor requirement were investigated.