Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 441, Issue 4, Pages 732-736Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2013.10.116
Keywords
Dissimilatory sulfite reductase; Desulfovibrio; DsrC; MalPEG; Gel-shift assay
Categories
Funding
- Fundacao para a Ciencia e Tecnologia (FCT, Portugal)
- Luso-German Joint Action [A-21/11]
- DAAD
- CRUP
- U.S. Department of Energy's Office of Biological and Environmental Research located at Pacific Northwest National Laboratory
- FCT, Portugal [SFRH/BPD/79823/2011]
- [PTDC/QUI-BIQ/100591/2008]
- [PTDC/BIA-PRO/098224/2008]
- [Pest-OE/EQB/LA0004/2011]
- Fundação para a Ciência e a Tecnologia [PEst-OE/EQB/LA0004/2011, SFRH/BPD/79823/2011] Funding Source: FCT
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Dissimilatory reduction of sulfite is carried out by the siroheme enzyme DsrAB, with the involvement of the protein DsrC, which has two conserved redox-active cysteines. DsrC was initially believed to be a third subunit of DsrAB. Here, we report a study of the distribution of DsrC in cell extracts to show that, in the model sulfate reducer Desulfovibrio vulgaris, the majority of DsrC is not associated with DsrAB and is thus free to interact with other proteins. In addition, we developed a cysteine-labelling gel-shift assay to monitor the DsrC redox state and behaviour, and procedures to produce the different redox forms. The oxidized state of DsrC with an intramolecular disulfide bond, which is proposed to be a key metabolic intermediate, could be successfully produced for the first time by treatment with arginine. (C) 2013 Elsevier Inc. All rights reserved.
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