The Redox State of the [2Fe-2S] Clusters in SoxR Protein Regulates Its Activity as a Transcription Factor
Open Access
- 1 December 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (52), 33173-33175
- https://doi.org/10.1074/jbc.271.52.33173
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form.Proceedings of the National Academy of Sciences, 1996
- Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein.Proceedings of the National Academy of Sciences, 1996
- Activation of SoxR-dependent Transcription in Vitro by Noncatalytic or NifS-mediated Assembly of [2Fe-2S[ Clusters into Apo-SoxRPublished by Elsevier ,1996
- Binuclear [2Fe-2S] Clusters in the Escherichia coli SoxR Protein and Role of the Metal Centers in TranscriptionPublished by Elsevier ,1995
- Overproduction and Physical Characterization of SoxR, a [2Fe-2S] Protein That Governs an Oxidative Response Regulon in Escherichia coliPublished by Elsevier ,1995
- Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages.Proceedings of the National Academy of Sciences, 1993
- Oxidized Redox State of Glutathione in the Endoplasmic ReticulumScience, 1992
- Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon.Proceedings of the National Academy of Sciences, 1992
- REGULATION OF BACTERIAL OXIDATIVE STRESS GENESAnnual Review of Genetics, 1991
- [23] Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systemsMethods in Enzymology, 1978