PMID:15898769

Citation	Cicchillo, RM, Tu, L, Stromberg, JA, Hoffart, LM, Krebs, C and Booker, SJ (2005) Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. J. Am. Chem. Soc. 127:7310-1
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.
Links	PubMed Online version:10.1021/ja051369x
Keywords	Azotobacter vinelandii/enzymology; Azotobacter vinelandii/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Dihydroxyacetone Phosphate/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; NADP/chemistry; NADP/metabolism; Plasmids; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Spectrophotometry, Ultraviolet; Spectroscopy, Mossbauer
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