Abstract：
: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 form, depressing the apparent pK by at least 2.5 pH units to a value of 7.3. Butyryl-, octanoyl-, and palmitoyl-CoA induce very similar spectral changes to those induced by enoyl-CoA derivatives when added anaerobically to the blue semiquinone enzyme. In contrast, the competitive inhibitors acetoacetyl-CoA and heptadecyl-SCoA do not markedly perturb the spectrum of the neutral flavosemiquinone species. The stability of the enzyme radical complexes with either crotonyl- or octanoyl-CoA suggests that there is not effective intraflavin transfer of reducing equivalents between subunits. Perturbation of the spectrum of the one-electron-reduced enzyme by ligands may complicate interpretation of the reaction enzyme by ligands may complicate interpretation of the reaction between substrate complexes of the general acyl-CoA dehydrogenase and electron-transferring flavoprotein.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Mizzer JP,Thorpe Cdoi
10.1021/bi00520a024subject
Has Abstractpub_date
1981-08-18 00:00:00pages
4965-70issue
17eissn
0006-2960issn
1520-4995journal_volume
20pub_type
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