title: Bromoperoxidases from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix.
abstract: The isolation and purification of bromoperoxidases from three marine subtropical green algae is described. In the presence of KBr and H2O2, each halide-specific enzyme catalyses the bromination of monochlorodimedone (2-chloro-5,5-dimethylcyclohexane-1,3-dione) to bromochlorodimedone (2-bromo-2-chloro-5,5-dimethylcyclohexane-1,3-dione). The enzymes also catalyse the oxidation of pyrogallol, o-phenylenediamine and I- to I3-. Preliminary characterization of these enzymes reveals acidic pH optima, high thermal stability, sensitivity to higher H2O2 concentrations, and apparent molecular weights ranging from 48000 to 60000.
mesh_terms: D001965:Bromides; D000460:Chlorophyta / Q000201:enzymology*; D003512:Cyclohexanones / Q000378:metabolism; D008970:Molecular Weight; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
chemical_list: D001965:Bromides; D003512:Cyclohexanones; C006991:chlorodimedone; D010544:Peroxidases; C026195:bromide peroxidase