Oxygenation of mitochondrial membranes by the erythroid lipoxygenase. Consequences for membrane properties.
The reticulocyte lipoxygenase is able to oxygenate mitochondrial membranes. The main products formed during this reaction are 15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid (15-HETE) and 13S-hydroperoxy-9Z,11E-octadecadienoic acid (13-HODE). The oxygenation of mitochondrial membranes is accompanied by an inactivation of enzymes localized in the outer and inner mitochondrial membranes, by a drastic change of the passive electric properties and by a destruction of the iron-sulfur clusters of the outer mitochondrial membrane. The possible mechanism of the processes leading to these functional changes is discussed.
Wiesner
R
R
Institute of Biochemistry, School of Medicine (Charité), Humboldt University, Berlin, GDR.
Kühn
H
H
Anton
M
M
Schewe
T
T
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D004789:Enzyme Activation; D005227:Fatty Acids / Q000378:metabolism; D007700:Kinetics; D008084:Lipoxygenase / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism; D051381:Rats; D012156:Reticulocytes / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet
D005227:Fatty Acids; D008084:Lipoxygenase; D008995:Monoamine Oxidase