Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein.
General acyl coenzyme A dehydrogenase from pig liver mitochondria, which was prepared as a complex with C8CoA and mixed with electron-transfer flavoprotein, rapidly reduces the electron-transfer flavoprotein to a 1-electron-reduced form (anionic semiquinone). A second electron is transferred more slowly to form the fully reduced electron-transfer flavoprotein. Transfer of the first electron is faster than turnover in the dichlorophenolindophenol reduction assay. These observations show that the acyl-CoA dehydrogenase-electron-transfer flavoprotein system utilizes this semiquinone catalytically. A concomitant appearance of semiquinone from the general acyl-CoA dehydrogenase could not be detected under similar conditions.
D044944:Acyl-CoA Dehydrogenases / Q000378:metabolism*; D000818:Animals; D004579:Electron Transport; D005420:Flavoproteins / Q000378:metabolism*; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry
D005420:Flavoproteins; D044944:Acyl-CoA Dehydrogenases