Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide.
Yellow butyryl-CoA dehydrogenase and general acyl-CoA dehydrogenase are "greened" by a mixture of coenzyme A plus elemental sulfur. The resultant stable complex contains an identical ligand with that present in native green butyryl-CoA dehydrogenase and has the same broad absorption band centered at 710 nm. Evidence is presented that the greening ligand is a CoA persulfide, possibly a mimic of the substrate carbanion thought to be generated early in the normal catalytic cycle. Variation in the position of the long wavelength band on replacement of FAD by a series of analogs of differing oxidation-reduction potential is consistent with a charge-transfer complex between a persulfide as the donor and oxidized flavin as the acceptor. The possible physiological and metabolic significance is discussed.
D044944:Acyl-CoA Dehydrogenases / Q000032:analysis*; D000818:Animals; D044926:Butyryl-CoA Dehydrogenase; D003065:Coenzyme A / Q000031:analogs & derivatives*; D005182:Flavin-Adenine Dinucleotide / Q000031:analogs & derivatives; D007668:Kidney / Q000201:enzymology; D008024:Ligands; D010462:Peptostreptococcus / Q000201:enzymology; D011485:Protein Binding; D013053:Spectrophotometry; D013552:Swine
D008024:Ligands; D005182:Flavin-Adenine Dinucleotide; D044944:Acyl-CoA Dehydrogenases; D044926:Butyryl-CoA Dehydrogenase; D003065:Coenzyme A