Williamson G, Engel P C, Mizzer J P, Thorpe C, Massey V
J Biol Chem. 1982 Apr 25;257(8):4314-20.
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.
黄色丁酰辅酶A脱氢酶和通用酰基辅酶A脱氢酶可被辅酶A与元素硫的混合物“绿化”。所得的稳定复合物含有与天然绿色丁酰辅酶A脱氢酶中存在的相同配体，并且具有以710nm为中心的相同宽吸收带。有证据表明，绿化配体是一种辅酶A过硫化物，可能是正常催化循环早期产生的底物碳负离子的模拟物。用一系列具有不同氧化还原电位的类似物取代FAD时，长波带位置的变化与以过硫化物作为供体和氧化黄素作为受体之间的电荷转移复合物一致。讨论了其可能的生理和代谢意义。
