The sources of inorganic sulfur in the process of cluster protein Fnr[4Fe-4S2+ reconstruction in Escherichia coli cells cultivated with NO-donating agents
Dinitrosyl iron complexes (DNICs) with thiol ligands--binuclear and mononuclear--inhibited aidB gene expression in E. coli cells. This process is due to the nitrosylation of the active center in iron-sulfur protein Fnr [4Fe-4S]2+ by low-molecular DNICs. The next step is transformation of the above D...
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Published in: | Biofizika Vol. 57; no. 2; p. 247 |
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Language: | Russian |
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Russia (Federation)
01-03-2012
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Abstract | Dinitrosyl iron complexes (DNICs) with thiol ligands--binuclear and mononuclear--inhibited aidB gene expression in E. coli cells. This process is due to the nitrosylation of the active center in iron-sulfur protein Fnr [4Fe-4S]2+ by low-molecular DNICs. The next step is transformation of the above DNICs into the DNICs with the thiol groups in the apo-form of Fnr protein. These nitrosylated proteins are characterized by the EPR signal with g perpendicular = 2.04 and g parallel 1 = 2,014. An addition of sulfur containing L-Cys or N-A-L-Cys as well as Na2S to the cells lead to the increasing in the aidB gene expression simultaneously with an appearance of the EPR signal with g perpendicular = 2.04 and g parallel = 2.02 as the characteristics of the DNICs with persulfide (R-S-S-) ligands. We suppose that the recovery of the aidB gene activity was due to the accumulation of inorganic sulfur in the cells and reconstruction of the active center in Fnr[4Fe-4S]2+. It appears that the above process is the function of L-cysteine-desulfurase protein which repaired the active center of Fnr[4Fe-4S]2+ protein using the sulfur from L-Cys or N-A-L-Cys after its deacetylation. On the other side the ions of inorganic sulfur being reacted with SH-groups led to the transformation of DNIC with thiol ligands into the persulfides. Na2S was the most potent activator of the aidB gene expression in our experiments. |
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AbstractList | Dinitrosyl iron complexes (DNICs) with thiol ligands--binuclear and mononuclear--inhibited aidB gene expression in E. coli cells. This process is due to the nitrosylation of the active center in iron-sulfur protein Fnr [4Fe-4S]2+ by low-molecular DNICs. The next step is transformation of the above DNICs into the DNICs with the thiol groups in the apo-form of Fnr protein. These nitrosylated proteins are characterized by the EPR signal with g perpendicular = 2.04 and g parallel 1 = 2,014. An addition of sulfur containing L-Cys or N-A-L-Cys as well as Na2S to the cells lead to the increasing in the aidB gene expression simultaneously with an appearance of the EPR signal with g perpendicular = 2.04 and g parallel = 2.02 as the characteristics of the DNICs with persulfide (R-S-S-) ligands. We suppose that the recovery of the aidB gene activity was due to the accumulation of inorganic sulfur in the cells and reconstruction of the active center in Fnr[4Fe-4S]2+. It appears that the above process is the function of L-cysteine-desulfurase protein which repaired the active center of Fnr[4Fe-4S]2+ protein using the sulfur from L-Cys or N-A-L-Cys after its deacetylation. On the other side the ions of inorganic sulfur being reacted with SH-groups led to the transformation of DNIC with thiol ligands into the persulfides. Na2S was the most potent activator of the aidB gene expression in our experiments. |
Author | Strel'tsova, D A Vanin, A F Vlaskina, A V Vasil'eva, S V Mikoian, V D |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22594280$$D View this record in MEDLINE/PubMed |
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Snippet | Dinitrosyl iron complexes (DNICs) with thiol ligands--binuclear and mononuclear--inhibited aidB gene expression in E. coli cells. This process is due to the... |
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SubjectTerms | Electron Spin Resonance Spectroscopy Escherichia coli - growth & development Escherichia coli - metabolism Escherichia coli Proteins - biosynthesis Escherichia coli Proteins - metabolism Gene Expression Regulation, Bacterial - drug effects Gene Expression Regulation, Bacterial - physiology Iron - metabolism Iron-Sulfur Proteins - metabolism Nitric Oxide Donors - pharmacology Nitrogen Oxides - metabolism Sulfides - metabolism Sulfides - pharmacology Sulfur - metabolism Sulfur - pharmacology |
Title | The sources of inorganic sulfur in the process of cluster protein Fnr[4Fe-4S2+ reconstruction in Escherichia coli cells cultivated with NO-donating agents |
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