The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii
Open Access
- 1 December 1971
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 125 (3) , 879-887
- https://doi.org/10.1042/bj1250879
Abstract
Butyryl-CoA dehydrogenase prepared by a simple procedure from Peptostreptococcus elsdenii has a molecular weight of approx. 150000. The enzyme has FAD as its prosthetic group. The amino acid analysis is reported. This enzyme, like most of the corresponding mammalian ones, is green. The absorption band at 710nm can be abolished irreversibly by dithionite reduction and air reoxidation; it can be abolished reversibly by phenylmercuric acetate or potassium bromide. The enzyme as isolated appears to be a mixture of a green and a yellow form, both of which are active. This view is supported by the variable ‘greenness’ of different preparations and the biphasic curve obtained in anaerobic spectrophotometric titrations with dithionite. It can be calculated from the titration results that fully green enzyme would have a peak-to-peak absorption ratio (E710/E430) as great as 0.54. The green form is much less rapidly reduced by dithionite than the yellow form, but is nevertheless much more readily reduced by dithionite than the enzyme from pig liver. It is also more readily reoxidized by air and shows less tendency to form a semiquinone. Treatment with sodium borohydride produces an unusual reduced species that is probably the 3,4-dihydroflavin.Keywords
This publication has 19 references indexed in Scilit:
- Green butyryl-coenzyme A dehydrogenase. An enzyme–acyl-coenzyme A complexBiochemical Journal, 1971
- Purification and characterization of flavodoxin from Peptostreptococcus elsdenii.1969
- On the Reaction of Borohydride with d- and l-Amino Acid OxidasesJournal of Biological Chemistry, 1968
- STUDIES ON CRYSTALLINE D-AMINO ACID OXIDASE .V. CHARACTERIZATION OF BOROHYDRIDE-REDUCED ENZYME-SUBSTRATE INTERMEDIATE SYNTHESIS OF EPSILON-N-(1-CARBOXYETHYL)-L-LYSINE1967
- The Electron-transferring Flavoprotein as a Common Intermediate in the Mitochondrial Oxidation of Butyryl Coenzyme A and SarcosineJournal of Biological Chemistry, 1966
- MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME-A .7. NATURE OF THE GREEN COLOR OF BUTYRYL DEHYDROGENASE1958
- MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME-A .1. GENERAL FATTY ACYL COENZYME A DEHYDROGENASE1956
- MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME-A .2. ELECTRON-TRANSFERRING FLAVOPROTEIN1956
- A new method for preparing flavin-adenine dinucleotideBiochemical Journal, 1953
- The coupled oxidation of pyruvate with glutathione and cysteineBiochemical Journal, 1951