The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria.
The topology of superoxide generation by sn-glycerol 3-phosphate dehydrogenase and complex III in intact Drosophila mitochondria was studied using aconitase inactivation to measure superoxide production in the matrix, and hydrogen peroxide formation in the presence of superoxide dismutase to measure superoxide production from both sides of the membrane. Aconitase inactivation was calibrated using the known rate of matrix superoxide production from complex I. Glycerol phosphate dehydrogenase generated superoxide about equally to each side of the membrane, whereas centre o of complex III in the presence of antimycin A generated superoxide about 30% on the cytosolic side and 70% on the matrix side.
Miwa
Satomi
S
MRC Dunn Human Nutrition Unit, Cambridge CB2 2XY, UK.
Brand
Martin D
MD
D000154:Aconitate Hydratase / Q000037:antagonists & inhibitors / Q000378:metabolism; D000818:Animals; D000968:Antimycin A; D004331:Drosophila melanogaster / Q000378:metabolism*; D014450:Electron Transport Complex III / Q000378:metabolism*; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D013053:Spectrophotometry; D013481:Superoxides / Q000378:metabolism*
D013481:Superoxides; D000968:Antimycin A; D006861:Hydrogen Peroxide; D005993:Glycerolphosphate Dehydrogenase; D000154:Aconitate Hydratase; D014450:Electron Transport Complex III