Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein.
نویسندگان
چکیده
منابع مشابه
Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase.
Middleton, €3. & Bartlett, K. (1983) C’lin. C’him. A m 128,291-305 Pullman, M. ( 1973) Ancil. Hiodwrn. 54, 188198 Reeve, D. R. & Crozier, A. ( 1977) J . C‘hromufogr. 137,27 1-282 Skredc. S. & Bremer. J . ( 1970) Eitr. J . Hiochem. 14,465-472 Stanley. K. K. & Tubbx. P. K. ( 1974) FEHS Lrrr. 39.325-328 Stanley. K. K. & Tubbs. P. K. (1975) Uioclirm. J . 150,77-88 Stewart, H. B., Tubbs, P. K. & Sta...
متن کاملCircular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein.
The flavin-protein interactions and flavoprotein-ligand interactions in the general acyl-CoA dehydrogenase from pig liver were studied by measuring the absorption spectra and circular dichroism spectra of the oxidized enzyme and complexes of the oxidized enzyme with enoyl-CoA products and two dead-end inhibitors. The spectra indicate that the flavin is slightly reoriented upon ligand binding an...
متن کاملCross-linking of the electron-transfer flavoprotein to electron-transfer flavoprotein-ubiquinone oxidoreductase with heterobifunctional reagents.
The mitochondrial electron-transfer flavoprotein (ETF) is a heterodimer containing only one FAD. In previous work on the structure-function relationships of ETF, its interaction with the general acyl-CoA dehydrogenase (GAD) was studied by chemical cross-linking with heterobifunctional reagents [D. J. Steenkamp (1987) Biochem. J. 243, 519-524]. GAD whose lysine residues were substituted with 3-(...
متن کاملSubunit structure of electron transfer flavoprotein.
The electron transfer flavoprotein from pig liver mitochondria is a 57,000-dalton electron transferase which links several primary flavoprotein dehydrogenases with the mitochondrial electron transport system. The protein was previously reported to be a dimer of apparently identical subunits. There are conflicting estimates in the literature regarding the FAD content of the protein. The results ...
متن کاملPartial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans.
Glutaryl-coenzyme A (CoA) dehydrogenase and the electron transfer flavoprotein (ETF) of Paracoccus denitrificans were purified to homogeneity from cells grown with glutaric acid as the carbon source. Glutaryl-CoA dehydrogenase had a molecular weight of 180,000 and was made up of four identical subunits with molecular weights of about 43,000 each of which contained one flavin adenine dinucleotid...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85743-5