Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: distinct differential sensitivity to superoxide-mediated signal transduction (Q41787082)

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scientific article published on 20 August 2012

Language	Label	Description	Also known as
English	Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: distinct differential sensitivity to superoxide-mediated signal transduction	scientific article published on 20 August 2012

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Direct oxidation of the [2Fe-2S] cluster in SoxR protein by superoxide: distinct differential sensitivity to superoxide-mediated signal transduction (English)

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

author name string

Mayu Fujikawa

1

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Kazuo Kobayashi

2

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Takahiro Kozawa

3

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

language of work or name

0 references

publication date

20 August 2012

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Europe PubMed Central

PMC publication ID

9 October 2017

number of pages

7

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

287

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

42

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

35702-35708

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

Protein Conformational Changes of the Oxidative Stress Sensor, SoxR, upon Redox Changes of the [2Fe–2S] Cluster Probed with Ultraviolet Resonance Raman Spectroscopy

1 reference

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The SoxRS response of Escherichia coli is directly activated by redox‐cycling drugs rather than by superoxide

1 reference

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Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase

1 reference

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Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA

1 reference

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DNA binding shifts the redox potential of the transcription factor SoxR

1 reference

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Cellular defenses against superoxide and hydrogen peroxide

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Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and independent transcriptional networks

1 reference

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Crystallization and preliminary X-ray crystallographic studies of the oxidative-stress sensor SoxR and its complex with DNA.

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Activation of SoxR-dependent transcription in Pseudomonas aeruginosa

1 reference

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Bacterial redox sensors.

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A reducing system of the superoxide sensor SoxR in Escherichia coli

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Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate

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Redox-operated genetic switches: the SoxR and OxyR transcription factors

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DNA distortion mechanism for transcriptional activation by ZntR, a Zn(II)-responsive MerR homologue in Escherichia coli

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Oxidative stress

1 reference

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In vivo kinetics of a redox-regulated transcriptional switch

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Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor

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Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo

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The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor.

1 reference

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SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form

1 reference

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DNA-bend modulation in a repressor-to-activator switching mechanism

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Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli

1 reference

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Identifiers

10.1074/JBC.M112.395079

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

9 October 2017

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