On the mechanism of lipoxygenase-like action of bleomycin-iron complexes.
The mechanism of lipid peroxidation catalyzed by bleomycin (BLM)-iron (Fe) complexes has been studied in vitro using sodium linoleate as a substrate. BLM-Fe(II)-O2 and BLM-Fe(III) complexes catalyze lipid peroxidation concomitantly with singlet oxygen evolution. The results from spin trapping methods and gas chromatography-mass spectroscopy (GCMS) analyses suggest that the initial step of lipid peroxidation catalyzed by BLM-Fe complexes is similar to that of soybean lipoxygenase, viz., hydrogen abstration. However, another mechanism might be concerned in the case of BLM-Fe(II)-O2 complex. BLM-Fe complexes are also capable of enhancing singlet oxygen evolution from the hydrogen peroxide (H2O2)-hypochlorite (OCl-) system.
Kikuchi
H
H
Department of Biochemistry II, Jichi Medical School, Tochigi-ken, Japan.
Tetsuka
T
T
D001761:Bleomycin / Q000737:chemistry* / Q000031:analogs & derivatives; D003497:Cyclic N-Oxides; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D007700:Kinetics; D008041:Linoleic Acids / Q000737:chemistry; D015227:Lipid Peroxidation; D008084:Lipoxygenase / Q000737:chemistry*; D008163:Luminescent Measurements; D010101:Oxygen Consumption; D010881:Piperidones; D013113:Spin Labels; D014216:Triacetoneamine-N-Oxyl / Q000031:analogs & derivatives
D003497:Cyclic N-Oxides; D008041:Linoleic Acids; D010881:Piperidones; D013113:Spin Labels; C023503:iron bleomycin; D001761:Bleomycin; D014216:Triacetoneamine-N-Oxyl; C002273:tempidon; C017245:5,5-dimethyl-1-pyrroline-1-oxide; D008084:Lipoxygenase