Details
| Original language | English |
|---|---|
| Pages (from-to) | 141-150 |
| Number of pages | 10 |
| Journal | AMINO ACIDS |
| Volume | 41 |
| Issue number | 1 |
| Publication status | Published - 1 Jun 2011 |
Abstract
Mobilization of the L-cysteine sulfur for the persulfuration of the rhodanese of Azotobacter vinelandii, RhdA, can be mediated by the A. vinelandii cysteine desulfurases, IscS and NifS. The amount of cysteine was higher in mutant strains lacking rhdA (MV474) than in wild type. The diazotrophic growth of MV474 was impaired. Taking into account the functional results about rhodanese-like proteins and RhdA itself, it is suggested that RhdA-dependent modulation of L-cysteine levels must deal with a redox-related process.
Keywords
- Azotobacter vinelandii, Cysteine desulfurase, L-Cysteine, RhdA, Sulfurtransferase, Thiosulfate
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
- Chemistry(all)
- Organic Chemistry
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In: AMINO ACIDS, Vol. 41, No. 1, 01.06.2011, p. 141-150.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Mobilization of sulfane sulfur from cysteine desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA
AU - Cartini, Francesca
AU - Remelli, William
AU - Santos, Patricia C.Dos
AU - Papenbrock, Jutta
AU - Pagani, Silvia
AU - Forlani, Fabio
N1 - Funding information: Mobility of researchers between Italy and Germany was sponsored by Vigoni project n. 0815171 (2009-2010; Ateneo Italo-Tedesco, Deutscher Akademischer Austausch Dienst) to FF and JP. FF was funded by “Fondo interno ricerca scientifica e tecnologica” (2005, 2006; Università degli Studi di Milano). We thank Eleonora di Paolo, Marco Pavoni and Dr. Aristodemo Carpen for skillful technical assistance. We also thank Prof. L.E. Vickery for providing E. coli IscS and Prof. D.R. Dean and Dr. D. Johnson for providing pDB943 and pDB551. C328A
PY - 2011/6/1
Y1 - 2011/6/1
N2 - Mobilization of the L-cysteine sulfur for the persulfuration of the rhodanese of Azotobacter vinelandii, RhdA, can be mediated by the A. vinelandii cysteine desulfurases, IscS and NifS. The amount of cysteine was higher in mutant strains lacking rhdA (MV474) than in wild type. The diazotrophic growth of MV474 was impaired. Taking into account the functional results about rhodanese-like proteins and RhdA itself, it is suggested that RhdA-dependent modulation of L-cysteine levels must deal with a redox-related process.
AB - Mobilization of the L-cysteine sulfur for the persulfuration of the rhodanese of Azotobacter vinelandii, RhdA, can be mediated by the A. vinelandii cysteine desulfurases, IscS and NifS. The amount of cysteine was higher in mutant strains lacking rhdA (MV474) than in wild type. The diazotrophic growth of MV474 was impaired. Taking into account the functional results about rhodanese-like proteins and RhdA itself, it is suggested that RhdA-dependent modulation of L-cysteine levels must deal with a redox-related process.
KW - Azotobacter vinelandii
KW - Cysteine desulfurase
KW - L-Cysteine
KW - RhdA
KW - Sulfurtransferase
KW - Thiosulfate
UR - http://www.scopus.com/inward/record.url?scp=79960413337&partnerID=8YFLogxK
U2 - 10.1007/s00726-010-0529-z
DO - 10.1007/s00726-010-0529-z
M3 - Article
C2 - 20213443
AN - SCOPUS:79960413337
VL - 41
SP - 141
EP - 150
JO - AMINO ACIDS
JF - AMINO ACIDS
SN - 0939-4451
IS - 1
ER -