• Journal Article

Isolation and characterization of a novel nonheme chloroperoxidase

Citation

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

Abstract

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.