Isolation and characterization of a novel nonheme chloroperoxidase
Chloroperoxidase, purified from the fermentation of Curvularia inaequalis, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (Mr 66,000). The enzyme was specific for I-, Br- and Cl-, and inactive toward F-. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no heme-like compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable.
Liu, T. N., M'Timkulu, T., Geigert, J., Wolf, B., Neidleman, S. L., Silva, D., & Hunter-Cevera, J. (1987). Isolation and characterization of a novel nonheme chloroperoxidase. Biochemical and Biophysical Research Communications, 142(2), 329-333. DOI: 10.1016/0006-291X(87)90277-4