We have reported that fatty-acid alpha-hydroxylase partially purified
from Sphingomonas paucimobilis required NADH and molecular oxygen. In
this study, we found that the reaction was greatly inhibited by catala
se. Glutathione and glutathione peroxidase also inhibited alpha-hydrox
ylation, but superoxide dismutase and mannitol did not. Replacement of
NADH and molecular oxygen by hydrogen peroxide increased the alpha-hy
droxylation activity. In the presence of hydrogen peroxide, molecular
oxygen was not required for the activity. These findings suggest that
hydrogen peroxide was essential for bacterial alpha-hydroxylase.