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

Journal Article · Fri Nov 29 04:00:00 EST 2013 · Biochemical and Biophysical Research Communications, 441(4):731-736

DOI:https://doi.org/10.1016/j.bbrc.2013.10.116· OSTI ID:1114105

Venceslau, Sofia S.; Cort, John R.; Baker, Erin Shammel; Chu, Rosalie K.; Robinson, Errol W.; Dahl, Christiane; Saraiva, Ligia M.; Pereira, Ines Ac

Dissimilatory reduction of sulfite is carried out by the siroheme enzyme DsrAB, with the involvement of the protein DsrC having two conserved cysteine residues. Here, we report a study of the distribution of DsrC in cell extracts, a cysteine-labelling gel-shift assay to monitor its redox state and behaviour, and procedures to produce the different redox forms. We 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 successfully produced DsrC with an intramolecular disulfide bond (oxidized state) by treatment with arginine.

• Research Organization: Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 1114105
• Report Number(s): PNNL-SA-98016; 35205; KP1704020
• Journal Information: Biochemical and Biophysical Research Communications, 441(4):731-736, Journal Name: Biochemical and Biophysical Research Communications, 441(4):731-736
• Country of Publication: United States
• Language: English

Related Subjects

Environmental Molecular Sciences Laboratory
NMR
structural genomics
structural biology