Stabilization of the red semiquinone form of pig kidney general acyl-CoA dehydrogenase by acyl coenzyme A derivatives.

  title={Stabilization of the red semiquinone form of pig kidney general acyl-CoA dehydrogenase by acyl coenzyme A derivatives.},
  author={J. Mizzer and C. Thorpe},
  volume={20 17},
Pig kidney general acyl-CoA dehydrogenases forms the blue neutral radical on dithionite or photochemical reduction (Thorpe, C., Matthews, R. G., & Williams, C. H. (1979) Biochemistry 18, 331-337] in accord with its classification as a flavoprotein dehydrogenase. However, dithionite reduction of the enzyme in the presence of crotonyl coenzyme A (crotonyl-CoA) or octenoyl-CoA generates the red radical anion as the predominant species at pH 7.6. Crotonyl-CoA binds preferentially to the red radical… Expand
Inactivation of general acyl-CoA dehydrogenase from pig kidney by 2-alkynoyl coenzyme A derivatives: initial aspects.
Both irreversible inactivation and covalent modification of the protein occur prior to the decay of the long wavelength species and these data are compared with the behavior of acyl-CoA dehydrogenases toward mechanism-based inactivators carrying an acetylene function at C-3, e.g., 3-butynoyl- CoA. Expand
The reductive half-reaction in Acyl-CoA dehydrogenase from pig kidney: studies with thiaoctanoyl-CoA and oxaoctanoyl-CoA analogues.
Data suggest that the enzyme can accomplish alpha-proton abstraction from certain weakly acidic acyl-CoA derivatives, without concerted transfer of a hydride equivalent to the flavin. Expand
Inactivation of two-electron reduced medium chain acyl-CoA dehydrogenase by 2-octynoyl-CoA.
Data suggest that a primary reduced flavin species undergoes various rearrangements during release from the protein, which is resistant to reoxidation using trans-2-octenoyl-CoA, molecular oxygen, or electron transferring flavoprotein. Expand
Acyl-CoA oxidase from Candida tropicalis.
Acyl coenzyme A oxidase (acyl-CoA oxidase) has been isolated in good yield from Candida tropicalis pK 233 grown on n-alkanes and measurement of flavin content suggest that the oxidase is an octamer of Mr 75 000 subunits each containing one flavin. Expand
Interflavin oxidation-reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron-transferring flavoprotein.
Rapid reaction and static fluorescence measurements showed that the final equilibrium mixture included appreciable levels of oxidized ETF and this was confirmed by measuring the reverse reactions. Expand
Oxidation-reduction of general acyl-CoA dehydrogenase by the butyryl-CoA/crotonyl-CoA couple. A new investigation of the rapid reaction kinetics.
A mechanism for the reduction/oxidation of GAD by butyryl- CoA/crotonyl-CoA was constructed and this mechanism was then used to simulate all of the observed kinetic time course data, using a single set of kinetic parameters. Expand
Alternate electron acceptors for medium-chain acyl-CoA dehydrogenase: use of ferricenium salts.
Evidence consistent with the presence of two distinct loci for redox communication with the bound flavin in the acyl-CoA dehydrogenase is presented, which may reflect the anticipated kinetic superiority of anionic flavin forms as reductants in outer-sphere electron-transfer processes. Expand
Acyl-CoA dehydrogenases. A mechanistic overview.
This work discusses the main factors that bring about catalysis, promote specificity and determine the selective transfer of electrons to electron transferring flavoprotein in medium chain acyl-CoA dehydrogenase. Expand
One-electron reduction of D-amino acid oxidase. Kinetics of conversion from the red semiquinone to the blue semiquinone.
The reduction of D-amino acid oxidase (DAAO) by hydrated electrons (eaq-) has been studied in the absence and presence of Benzoate by pulse radiolysis and the rate was found to be identical with that of the formation of the complex between benzoate and the red semiquinone of DAAO as measured by a stopped-flow method. Expand
Spectral and electrochemical properties of glutaryl-CoA dehydrogenase from Paracoccus denitrificans.
Studies of the spectral (UV/vis and resonance Raman) and electrochemical properties of the FAD-containing enzyme glutaryl-CoA dehydrogenase (GCD) from Paracoccus denitrificans reveal that theExpand