The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria.

TitleThe topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophila mitochondria.
Publication TypeJournal Article
Year of Publication2005
AuthorsMiwa, S, Brand, MD
JournalBiochim Biophys Acta
Volume1709
Issue3
Pagination214-9
Date Published2005 Sep 30
ISSN0006-3002
KeywordsAconitate Hydratase, Animals, Antimycin A, Drosophila melanogaster, Electron Transport Complex III, Glycerolphosphate Dehydrogenase, Hydrogen Peroxide, Mitochondria, Spectrophotometry, Superoxides
Abstract

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.

DOI10.1016/j.bbabio.2005.08.003
Alternate JournalBiochim. Biophys. Acta
Citation Key10.1016/j.bbabio.2005.08.003
PubMed ID16140258