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- W2034290296 abstract "The [2Fe–2S] transcription factor, SoxR, a member of the MerR family, functions as a bacterial sensor of oxidative stress in Escherichia coli. SoxR is activated by reversible one-electron oxidation of the [2Fe–2S] cluster and enhances the production of various antioxidant proteins through the SoxRS regulon. Ultraviolet resonance Raman (UVRR) spectroscopic analysis of SoxR revealed conformational changes upon reduction of the [2Fe–2S] cluster in the absence and presence of promoter oligonucleotide. UVRR spectra reflected the environmental or structural changes of Trp following reduction. Notably, the environment around Trp91 contacting the [2Fe–2S] cluster was altered to become more hydrophilic, whereas that around Trp98 exhibited a small change to become more hydrophobic. In addition, changes in cation−π interactions between the [2Fe–2S] cluster and Trp91 were suggested. On the other hand, the environment around Tyr was barely affected by the [2Fe–2S] reduction. Binding of the promoter oligonucleotide triggered changes in Tyr located in the DNA-binding domain, but not Trp. Furthermore, conformational changes induced upon reduction of DNA-bound SoxR were not significantly different from those of DNA-free SoxR." @default.
- W2034290296 created "2016-06-24" @default.
- W2034290296 creator A5012095999 @default.
- W2034290296 creator A5072098775 @default.
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- W2034290296 date "2011-10-17" @default.
- W2034290296 modified "2023-10-08" @default.
- W2034290296 title "Protein Conformational Changes of the Oxidative Stress Sensor, SoxR, upon Redox Changes of the [2Fe–2S] Cluster Probed with Ultraviolet Resonance Raman Spectroscopy" @default.
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- W2034290296 doi "https://doi.org/10.1021/bi201526y" @default.
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