Electron transfer flavoprotein (ETF, a heterodimer) transfers electrons from a variety of matrix acyl-CoA dehydrogenases to the respiratory chain through electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO). In assays performed after incubation of lipid peroxidation by-product 4-hydroxy-2-nonenal (4-HNE) with ETF, a 20% loss in activity is observed. Western blots show characteristic a and � subunits for unmodified ETF. Double subunit bands are observed at twice the molecular weight (MW) for ETF incubated with 4-HNE. MALDI-MS of unmodified ETF show distinct � (27.4 kD) and a (33 kD) bands with a broad band at 60-64 kD. MALDI-MS spectra of ETF/4-HNE suggest that subunit MWs increase to 29 kD and 34 kD. Evidence for modification of ETF by 4-HNE may be a significant factor in the pathophysiology of glutaric academia type II due to ETF-QO deficiency. In these situations reduced ETF can react directly with molecular oxygen to generate reactive oxygen species involved in the generation of 4-HNE.

Effects of 4-hydroxy-2-nonenal on electron transfer flavoprotein

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.