Crane 1956 J Biol Chem
| Crane FL, Beinert H (1956) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transferring flavoprotein. J Biol Chem 218:717-31. |
Crane FL, Beinert H (1956) J Biol Chem
Abstract: The preparation and some properties of a new flavoprotein (ETF) which specifically catalyzes the oxidation of the reduced forms of the green and the yellow fatty acyl CoA dehydrogenases by indophenol, ferricyanide, or cytochrome c are described. The prosthetic group of ETF appears to be FAD. The riboflavin content of ETF is 0.45 per cent, and its minimal molecular weight is 83,500 according to this flavin content. The ability of ETF to interact with cytochrome c is very variable, in contrast to the consistent interaction with other electron acceptors. This variability can be account.ed for in terms of protein interactions which occur in ETF preparat,ions and which arc reversed under specific conditions. The implications of the present work are discussed with respect to flavoprotein catalysis and electron transfer in general and with respect to the significance of cytochrome c as natural electron acceptor in the present system and the role of copper in butyryl CoA dehydrogenase.
• Bioblast editor: Gnaiger E
Selected quote
- 'The present investigation has established the principle that flavoproteins may operate in series in hydrogen or electron transfer. The accompanying scheme represents our present picture of hydrogen or electron transport in the enzymatic dehydrogenation of fatty acyl derivatives of CoA. The mechanism by which an oxidation-reduction can take place between proteins which have tightly bound prosthetic groups deserves interest.'
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