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- Title
Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.
- Authors
Serrano, Pauline N.; Wang, Hongxin; Crack, Jason C.; Prior, Christopher; Hutchings, Matthew I.; Thomson, Andrew J.; Kamali, Saeed; Yoda, Yoshitaka; Zhao, Jiyong; Hu, Michael Y.; Alp, Ercan E.; Oganesyan, Vasily S.; Le Brun, Nick E.; Cramer, Stephen P.
- 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, [Fe2(NO)4(Cys)2]) and Roussin's Black Salt (RBS, [Fe4(NO)7S3]. In the latter case, the absence of 32S/34S 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.
- Subjects
IRON sulfides; NITROSYLATION; NITRIC oxide; PROTEIN analysis; DENSITY functional theory; THIOLATES; VIBRATIONAL spectra
- Publication
Angewandte Chemie, 2016, Vol 128, Issue 47, p14795
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201607033