Studies of inhibitor binding to the [4Fe-4S] cluster of quinolinate synthase |
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| Authors: | Chan Alice Clémancey Martin Mouesca Jean-Marie Amara Patricia Hamelin Olivier Latour Jean-Marc Ollagnier de Choudens Sandrine |
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| Institution: | Laboratoire de Chimie de Biologie des Métaux, UMR 5249, Université Joseph Fourier, Grenoble-1, CNRS-CEA 17, Rue des Martyrs, 38054 Grenoble Cedex 9, France. |
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| Abstract: | Stop for NadA! A 4Fe-4S] enzyme, NadA, catalyzes the formation of quinolinic acid in de?novo nicotinamide adenine dinucleotide (NAD) biosynthesis. A structural analogue of an intermediate, 4,5-dithiohydroxyphthalic acid (DTHPA), has an in?vivo NAD biosynthesis inhibiting activity in E. coli. The inhibitory effect can be explained by the coordination of DTHPA thiolate groups to a unique Fe site of the NadA 4Fe-4S] cluster. |
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| Keywords: | inhibitors iron‐sulfur clusters Moessbauer spectroscopy NAD quinolinate |
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