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

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

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
Volume127
Issue number20
DOIs
StatePublished - May 25 2005

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Quinolinic Acid
Ports and harbors
Escherichia coli
Acids
Dihydroxyacetone Phosphate
Niacinamide
Polypeptides
Biosynthesis
Sulfides
Oxidation-Reduction
Paramagnetic resonance
Condensation
Spectrum Analysis
Phosphates
Iron
Genes
Spectroscopy
Proteins
Peptides
quinolinic acid synthetase

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Cicchillo, Robert M. ; Tu, Loretta ; Stromberg, Jeffrey A. ; Hoffart, Lee M. ; Krebs, Carsten ; Booker, Squire J. / Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. In: Journal of the American Chemical Society. 2005 ; Vol. 127, No. 20. pp. 7310-7311.
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abstract = "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, M{\"o}ssbauer, 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.",
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Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. / Cicchillo, Robert M.; Tu, Loretta; Stromberg, Jeffrey A.; Hoffart, Lee M.; Krebs, Carsten; Booker, Squire J.

In: Journal of the American Chemical Society, Vol. 127, No. 20, 25.05.2005, p. 7310-7311.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster

AU - Cicchillo, Robert M.

AU - Tu, Loretta

AU - Stromberg, Jeffrey A.

AU - Hoffart, Lee M.

AU - Krebs, Carsten

AU - Booker, Squire J.

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AB - 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.

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