Abstract
Dinitrosyl iron complexes (DNICs) with various thiol ligands, the known donors of nitric oxide, markedly inhibited aidB gene expression in E. coli cells by destroying the [4Fe-4S]2+ center of its regulator protein Fnr. Therewith, the cells accumulated DNICs in the protein-bound form, identified by the EPR signal with g⊥ = 2.04 and g‖ = 2.014. Subsequent addition of sulfur sources L-cysteine or N-acetylcysteine, DTT as well as Na2S to the DNIC-treated cells significantly restored the reporter gene expression. Simultaneously, the above-specified EPR signal was partly or completely replaced with a narrower signal (g⊥ = 2.032, g‖ = 2.02) identical to that of DNICs with persulfide (R-S-S−) ligands, which result from interaction of S2− with thiols; inorganic sulfide proved to be the most efficient agent. These data corroborate the central role of S2− in recovery of the protein [4Fe-4S] center disrupted by the NO donors.
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