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Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.
- Source :
- Angewandte Chemie; 11/14/2016, Vol. 128 Issue 47, p14795-14799, 5p
- Publication Year :
- 2016
-
Abstract
- The reaction of protein-bound iron-sulfur (Fe-S) clusters with nitric oxide (NO) plays key roles in NO-mediated toxicity and signaling. Elucidation of the mechanism of the reaction of NO with DNA regulatory proteins that contain Fe-S clusters has been hampered by a lack of information about the nature of the iron-nitrosyl products formed. Herein, we report nuclear resonance vibrational spectroscopy (NRVS) and density functional theory (DFT) calculations that identify NO reaction products in WhiD and NsrR, regulatory proteins that use a [4Fe-4S] cluster to sense NO. This work reveals that nitrosylation yields multiple products structurally related to Roussin's Red Ester (RRE, [Fe<subscript>2</subscript>(NO)<subscript>4</subscript>(Cys)<subscript>2</subscript>]) and Roussin's Black Salt (RBS, [Fe<subscript>4</subscript>(NO)<subscript>7</subscript>S<subscript>3</subscript>]. In the latter case, the absence of <superscript>32</superscript>S/<superscript>34</superscript>S shifts in the Fe−S region of the NRVS spectra suggest that a new species, Roussin's Black Ester (RBE), may be formed, in which one or more of the sulfide ligands is replaced by Cys thiolates. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00448249
- Volume :
- 128
- Issue :
- 47
- Database :
- Complementary Index
- Journal :
- Angewandte Chemie
- Publication Type :
- Academic Journal
- Accession number :
- 119459335
- Full Text :
- https://doi.org/10.1002/ange.201607033