Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 4314-4320 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 257 |
| Issue number | 8 |
| Publication status | Published - 25 Apr 1982 |
| Externally published | Yes |
Cite this
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Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide. / Williamson, G.; Engel, P. C.; Mizzer, J. P.; Thorpe, C.; Massey, V.
In: Journal of Biological Chemistry, Vol. 257, No. 8, 25.04.1982, p. 4314-4320.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide.
AU - Williamson, G.
AU - Engel, P. C.
AU - Mizzer, J. P.
AU - Thorpe, C.
AU - Massey, V.
PY - 1982/4/25
Y1 - 1982/4/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0020490576&partnerID=8YFLogxK
M3 - Article
VL - 257
SP - 4314
EP - 4320
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 1083-351X
IS - 8
ER -