1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough

• Published in: Biomolecular NMR assignments Vol. 5; no. 2; pp. 177 - 179
• Main Authors: Garcin, Edwige B., Bornet, Olivier, Pieulle, Laetitia, Guerlesquin, Françoise, Sebban-Kreuzer, Corinne
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.10.2011
• Subjects: Bacterial Proteins - chemistry; Biochemistry; Biological and Medical Physics; Biophysics; Desulfovibrio vulgaris - chemistry; Isotopes - chemistry; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Physics; Physics and Astronomy; Polymer Sciences; Recombinant Proteins - chemistry; Thioredoxins - chemistry; Hildenborough; Anaerobic bacteria; NMR; Thioredoxin
• ISSN: 1874-2718; 1874-270X; 1874-270X
• DOI: 10.1007/s12104-011-9294-5

Thioredoxins are ubiquitous key antioxidant enzymes which play an essential role in cell defense against oxidative stress. They maintain the redox homeostasis owing to the regulation of thiol-disulfide exchange. In the present paper, we report the full resonance assignments of 1 H, 13 C and 15 N atoms for the reduced and oxidized forms of Desulfovibrio vulgaris Hildenborough thioredoxin 1 (Trx1). 2D and 3D heteronuclear NMR experiments were performed using uniformly 15 N-, 13 C-labelled Trx1. Chemical shifts of 97% of the backbone and 90% of the side chain atoms were obtained for the oxidized and reduced form (BMRB deposits with accession number 17299 and 17300, respectively).