Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster

Robert M. Cicchillo, Loretta Tu, Jeffrey A. Stromberg, Lee M. Hoffart, Carsten Krebs, Squire J. Booker

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Quinolinic acid is an intermediate in the biosynthesis of nicotinamide-containing redox cofactors. The ultimate step in the formation of quinolinic acid in prokaryotes is the condensation of iminosuccinate and dihydroxyacetone phosphate, which is catalyzed by the product of the nadA gene in Escherichia coli. A combination of UV-vis, Mössbauer, and EPR spectroscopies, along with analytical methods for the determination of iron and sulfide, demonstrates for the first time that anaerobically purified quinolinate synthetase (NadA) from E. coli contains one [4Fe-4S] cluster per polypeptide. The protein is active, catalyzing the formation of quinolinic acid with a Vmax [ET]-1 of 0.01 s-1.

Original languageEnglish (US)
Pages (from-to)7310-7311
Number of pages2
JournalJournal of the American Chemical Society
Issue number20
StatePublished - May 25 2005

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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