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Nitrosylation of Nitric‐Oxide‐Sensing Regulatory Proteins Containing [4Fe‐4S] Clusters Gives Rise to Multiple Iron–Nitrosyl Complexes
Author(s) -
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.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201607033
Subject(s) - chemistry , density functional theory , nitrosylation , cluster (spacecraft) , sulfide , sulfur , nitric oxide , salt (chemistry) , iron–sulfur cluster , crystallography , photochemistry , computational chemistry , organic chemistry , enzyme , computer science , programming language
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 2 (NO) 4 (Cys) 2 ]) and Roussin's Black Salt (RBS, [Fe 4 (NO) 7 S 3 ]. In the latter case, the absence of 32 S/ 34 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.