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

doi:10.1021/ja051369x

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 journal › Article › peer-review

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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, 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 V_max [E_T]^-1 of 0.01 s^-1.

Original language	English (US)
Pages (from-to)	7310-7311
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	20
DOIs	https://doi.org/10.1021/ja051369x
State	Published - May 25 2005

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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title = "Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster",

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.",

author = "Cicchillo, {Robert M.} and Loretta Tu and Stromberg, {Jeffrey A.} and Hoffart, {Lee M.} and Carsten Krebs and Booker, {Squire J.}",

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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.

PY - 2005/5/25

Y1 - 2005/5/25

N2 - 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.

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

Abstract

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