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The spectroscopic data revealed that the coordination environments of the metal active centers varied only very slightly between the reduced and oxidized states, similar to most other proteins containing iron\u2013sulfur clusters. Upon nitrosylation of oxidized SoxR, however, we observed a low\u2010temperature EPR spectrum characteristic of a protein dinitrosyl iron complex (DNIC), with an intensity corresponding to about two DNICs per iron sulfur cluster in the protein, according to spin quantification relative to a low\u2010molecular\u2010weight DNIC standard. In addition, there was no evidence for dichroic spectral features in the responsive region of the nitrosyl iron complexes, as well as for Fe\uf8ffFe back\u2010scattering in the fitting of the Fe extended X\u2010ray absorption fine structure (EXAFS) spectrum. Instead the Fe EXAFS spectrum of the nitrosylated SoxR core exhibited the same first\u2010 and second\u2010shell coordination environments characteristic of modeled small molecular DNICs, indicating that each of the [2\u2009Fe\uf8ff2\u2009S] cores in the homodimeric SoxR was dissociated into two individual DNICs. Similar nitrosylation of the reduced mixed\u2010valence SoxR for 1\u2005min led to degradation of the iron\u2013sulfur clusters to give several iron species, including one with EPR signals characteristic of a reduced Roussin\u2019s red ester (rRRE), a diamagnetic species, presumably Roussin\u2019s red ester (RRE), and a small amount of DNIC. We also undertook in vivo time\u2010course studies of <jats:italic>E. coli<\/jats:italic> cells containing recombinant SoxR after rapid purging of the cells with exogenous NO gas. Rapid freeze\u2010quenched EPR experiments demonstrated rapid formation of the SoxR rRRE species, followed by fast breakup of this precursor intermediate to form the stable protein\u2010bound DNIC species. Accordingly, under nitrosative stress, we believe that the response of SoxR to NO could depend on the intracellular redox state of <jats:italic>E. coli<\/jats:italic>, the central modulator of which could be exploited to deduce the appropriate mechanism to sense the presence of NO for physiological regulation.<\/jats:p>","DOI":"10.1002\/chem.201100838","type":"journal-article","created":{"date-parts":[[2012,1,20]],"date-time":"2012-01-20T11:13:00Z","timestamp":1327057980000},"page":"2565-2577","source":"Crossref","is-referenced-by-count":27,"title":["The Metal Core Structures in the Recombinant <i>Escherichia coli<\/i> Transcriptional Factor 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