Purification and properties of peroxidase from Nitrosomonas europaea.

@article{Anderson1968PurificationAP,
  title={Purification and properties of peroxidase from Nitrosomonas europaea.},
  author={John A. Anderson and D H Strumeyer and David Pramer},
  journal={Journal of bacteriology},
  year={1968},
  volume={96 1},
  pages={93-7}
}
Peroxidase from the obligate chemosynthetic bacterium Nitrosomonas europaea was purified 1,500-fold, and its properties were examined. The enzyme had a molecular weight of 53,000 and exhibited characteristic absorption maxima at 410, 524, and 558 mmu. The optimal pH and temperature were 7.5 and 44 C, respectively. The peroxidase reaction had an energy of activation of 5,850 cal/mole and required a primary substrate (H(2)O(2)) concentration of 7 x 10(-6)m to proceed at half maximal velocity (K(m… CONTINUE READING