Bromoperoxidases from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix.
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.
D001965:Bromides; D000460:Chlorophyta / Q000201:enzymology*; D003512:Cyclohexanones / Q000378:metabolism; D008970:Molecular Weight; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
D001965:Bromides; D003512:Cyclohexanones; C006991:chlorodimedone; D010544:Peroxidases; C026195:bromide peroxidase