One-electron reduction of chloroperoxidase by radiolytically generated electrons.
Upon irradiation of aqueous ethylene glycol/water solutions of native chloroperoxidase (CPO) with 60Co-gamma rays at 77K one observes the one-electron reduction of the enzyme active site by radiolytically generated thermolyzed electrons. In the present study the first absorption spectrum of a low-spin ferrous form of CPO is reported which has peaks at 438, 532 and 563 nm, similar to those observed previously for cytochrome P-450. All previously described ferrous forms of CPO are high spin. In order to observe the final results of the CPO reaction with electrons, the spectral changes of native enzyme after room temperature-gamma-irradiation have also been investigated. Evidence of changes is also presented probably connected with disruption of the tertiary structure of enzyme, correlated with decrease of enzyme activity.
Metodiewa
D
D
Institute of Applied Radiation Chemistry, Technical University of Lodz, Poland.
Dunford
H B
HB
D002711:Chloride Peroxidase / Q000528:radiation effects*; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis; D004579:Electron Transport; D005720:Gamma Rays; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000528:radiation effects*; D013053:Spectrophotometry; D013696:Temperature
D003577:Cytochrome P-450 Enzyme System; D010544:Peroxidases; D002711:Chloride Peroxidase