Coenzyme A thiosulfonate (coenzyme A disulfide-S,S-dioxide), an affinity analog of coenzyme A.

J. S. Nishimura, T. Mitchell, K. A. Hill, G. E. Collier

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8 Scopus citations


The structure of the CoA affinity analog-oxidized CoA disulfide (o-CoAS2) (Collier, G. E., and Nishimura, J. S. (1978) J. Biol. Chem. 253, 4938-4939) has been deduced to be that of the thiosulfonate of CoA, i.e. coenzyme A disulfide-S,S-dioxide. This deduction is based on several considerations among which are: the cleavage of o-CoAS2 by dithiothreitol under anaerobic conditions to equimolar amounts of CoASH and CoASO2H; the alkali-catalyzed dismutation of 3 mol of o-CoAS2 to 4 mol of CoASO2H and 1 mol of CoA disulfide; and comparison of the 13C-NMR spectra of CoA disulfide and o-CoAS2. The results of studies with Clostridial phosphotransacetylase (EC and pigeon muscle carnitine acetyltransferase (EC were consistent with the action of o-CoAS2 as a CoA affinity analog on these enzymes. Inactivation was characterized by what appeared to be disulfide bonding between CoA and important sulfhydryl groups of the proteins.

Original languageEnglish (US)
Pages (from-to)14896-14902
Number of pages7
JournalJournal of Biological Chemistry
Issue number24
StatePublished - Dec 25 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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