CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase.

@article{Shaw1987CoApersulphideAP,
  title={CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase.},
  author={Lee Shaw and Paul C. Engel},
  journal={Biochimica et biophysica acta},
  year={1987},
  volume={919 2},
  pages={171-4}
}
The characteristic green colour of native short-chain acyl-CoA dehydrogenases (EC 1.3.99.2) results from a charge transfer complex between the FAD prosthetic group and a tightly bound molecule of CoA-persulphide. The native enzyme from ox liver mitochondria was found to have about 60% of its FAD cofactor liganded with CoA-persulphide. When artificially fully liganded with CoA-persulphide, this enzyme was inhibited by 90% in comparison to unliganded enzyme. Enzymic activity could be slowly… CONTINUE READING