期刊
AMINO ACIDS
卷 41, 期 1, 页码 141-150出版社
SPRINGER WIEN
DOI: 10.1007/s00726-010-0529-z
关键词
RhdA; Sulfurtransferase; Cysteine desulfurase; L-Cysteine; Thiosulfate; Azotobacter vinelandii
资金
- Ateneo Italo-Tedesco, Deutscher Akademischer Austausch Dienst [0815171]
- Fondo interno ricerca scientifica e tecnologica (Universita degli Studi di Milano)
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.
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