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Title: Redox states of Desulfovibrio vulgaris DsrC, a key protein in dissimilatory sulfite reduction

Highlights: •DsrC is known to interact with the dissimilatory sulfite reductase enzyme (DsrAB). •We show that, however, most cellular DsrC is not associated with DsrAB. •A gel-shift assay was developed that allows monitoring of the DsrC redox state. •The DsrC intramolecularly oxidized state could only be produced by arginine treatment. -- Abstract: 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.
Authors:
 [1] ; ;  [2] ; ;  [3] ;  [4] ;  [1] ;  [1]
  1. Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras (Portugal)
  2. Fundamental and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352 (United States)
  3. Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352 (United States)
  4. Institut für Mikrobiologie and Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn (Germany)
Publication Date:
OSTI Identifier:
22242203
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 441; Journal Issue: 4; Other Information: Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ARGININE; CYSTEINE; DESULFOVIBRIO; DISULFIDES; ENZYMES; GELS; LABELLING; SULFATES; SULFITES